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P00183

- CPXA_PSEPU

UniProt

P00183 - CPXA_PSEPU

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Protein

Camphor 5-monooxygenase

Gene

camC

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Involved in a camphor oxidation system.

Catalytic activityi

+-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O.

Cofactori

Heme group.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi358 – 3581Iron (heme axial ligand)

GO - Molecular functioni

  1. camphor 5-monooxygenase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. (+)-camphor catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3021.
UniPathwayiUPA00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Camphor 5-monooxygenase (EC:1.14.15.1)
Alternative name(s):
Cytochrome P450-cam
Short name:
Cytochrome P450cam
Gene namesi
Name:camC
Synonyms:cyp101
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 415414Camphor 5-monooxygenasePRO_0000052204Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-29809N.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83
Helixi21 – 233
Beta strandi29 – 313
Helixi35 – 373
Helixi39 – 435
Helixi44 – 474
Beta strandi48 – 514
Beta strandi53 – 575
Helixi59 – 613
Beta strandi63 – 664
Helixi69 – 779
Turni79 – 813
Beta strandi82 – 865
Beta strandi88 – 903
Helixi91 – 966
Turni100 – 1034
Turni106 – 1083
Helixi109 – 12012
Helixi122 – 14322
Helixi144 – 1463
Beta strandi147 – 1504
Helixi151 – 1544
Turni155 – 1573
Helixi158 – 16811
Helixi172 – 1743
Helixi175 – 18612
Beta strandi190 – 1923
Helixi194 – 21421
Helixi220 – 2256
Beta strandi230 – 2334
Helixi236 – 25116
Helixi253 – 26614
Helixi269 – 2779
Helixi279 – 2813
Helixi282 – 29211
Beta strandi298 – 3047
Beta strandi306 – 3083
Beta strandi311 – 3133
Beta strandi318 – 3214
Helixi323 – 3286
Turni330 – 3323
Beta strandi333 – 3353
Helixi354 – 3563
Helixi361 – 37818
Beta strandi382 – 3843
Beta strandi395 – 3973
Beta strandi399 – 4013
Beta strandi404 – 4063
Helixi409 – 4113

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKDX-ray1.80A2-415[»]
1C8JX-ray2.10A/B2-415[»]
1CP4X-ray1.90A2-415[»]
1DZ4X-ray1.60A/B2-415[»]
1DZ6X-ray1.90A/B2-415[»]
1DZ8X-ray1.90A/B2-415[»]
1DZ9X-ray1.90A/B2-415[»]
1GEBX-ray2.03A1-415[»]
1GEKX-ray1.70A1-415[»]
1GEMX-ray2.00A1-415[»]
1GJMX-ray2.20A2-415[»]
1IWIX-ray2.00A1-415[»]
1IWJX-ray2.00A1-415[»]
1IWKX-ray2.00A1-415[»]
1J51X-ray2.20A/B/C/D2-415[»]
1K2OX-ray1.65A/B2-415[»]
1LWLX-ray2.20A1-415[»]
1MPWX-ray2.34A/B2-415[»]
1NOOX-ray2.20A2-415[»]
1O76X-ray1.80A/B2-415[»]
1P2YX-ray2.30A2-415[»]
1P7RX-ray2.85A2-415[»]
1PHAX-ray1.63A2-415[»]
1PHBX-ray1.60A2-415[»]
1PHCX-ray1.60A2-415[»]
1PHDX-ray1.60A2-415[»]
1PHEX-ray1.60A2-415[»]
1PHFX-ray1.60A2-415[»]
1PHGX-ray1.60A2-415[»]
1QMQX-ray1.55A2-415[»]
1RE9X-ray1.45A2-415[»]
1RF9X-ray1.80A1-415[»]
1T85X-ray1.80A2-415[»]
1T86X-ray1.90A/B2-415[»]
1T87X-ray1.80A/B2-415[»]
1T88X-ray1.90A/B2-415[»]
1UYUX-ray2.00A/B2-415[»]
1YRCX-ray1.40A2-415[»]
1YRDX-ray1.70A2-415[»]
2A1MX-ray2.10A/B1-415[»]
2A1NX-ray1.90A/B1-415[»]
2A1OX-ray1.55A/B1-415[»]
2CP4X-ray2.10A2-415[»]
2CPPX-ray1.63A2-415[»]
2FE6X-ray1.50A1-415[»]
2FERX-ray1.70A11-415[»]
2FEUX-ray1.70A/B11-415[»]
2FRZX-ray2.10A/B2-415[»]
2GQXX-ray2.10A/B11-415[»]
2GR6X-ray2.30A/B11-415[»]
2H7QX-ray1.50A2-415[»]
2H7RX-ray2.10A2-415[»]
2H7SX-ray2.15A/C2-415[»]
2L8MNMR-A1-415[»]
2LQDNMR-A11-415[»]
2M56NMR-A12-415[»]
2QBLX-ray1.80A1-415[»]
2QBMX-ray1.80A1-415[»]
2QBNX-ray1.75A1-415[»]
2QBOX-ray1.90A1-415[»]
2Z97X-ray1.80A1-415[»]
2ZAWX-ray1.55A1-415[»]
2ZAXX-ray1.60A1-415[»]
2ZUHX-ray1.55A1-415[»]
2ZUIX-ray1.50A1-415[»]
2ZUJX-ray1.60A1-415[»]
2ZWTX-ray1.35A1-415[»]
2ZWUX-ray1.30A1-415[»]
3CP4X-ray2.30A2-415[»]
3CPPX-ray1.90A2-415[»]
3FWFX-ray1.83A/B11-415[»]
3FWGX-ray1.55A/B11-415[»]
3FWIX-ray2.40A11-415[»]
3FWJX-ray1.90A11-415[»]
3L61X-ray1.50A2-415[»]
3L62X-ray1.70A2-415[»]
3L63X-ray1.50A2-415[»]
3OIAX-ray1.65A2-415[»]
3OL5X-ray1.75A2-415[»]
3P6MX-ray2.00A2-415[»]
3P6NX-ray1.70A2-415[»]
3P6OX-ray2.00A2-415[»]
3P6PX-ray1.90A2-415[»]
3P6QX-ray1.95A2-415[»]
3P6RX-ray2.10A2-415[»]
3P6SX-ray2.00A2-415[»]
3P6TX-ray1.90A2-415[»]
3P6UX-ray1.70A2-415[»]
3P6VX-ray2.00A2-415[»]
3P6WX-ray2.10A2-415[»]
3P6XX-ray1.65A2-415[»]
3W9CX-ray2.50A2-415[»]
4CP4X-ray2.10A2-415[»]
4CPPX-ray2.11A2-415[»]
4EK1X-ray1.97A/B2-415[»]
4G3RX-ray2.20A/B2-415[»]
4JWSX-ray2.15A/B1-415[»]
4JWUX-ray2.20A/B1-415[»]
4JX1X-ray2.09A/B/E/F1-415[»]
4KKYX-ray2.00X2-414[»]
4L49X-ray2.13A1-415[»]
4L4AX-ray2.10A1-415[»]
4L4BX-ray2.10A1-415[»]
4L4CX-ray2.20A/B1-415[»]
4L4DX-ray2.10A1-415[»]
4L4EX-ray1.26A1-415[»]
4L4FX-ray1.29A1-415[»]
4L4GX-ray1.55A1-415[»]
5CP4X-ray1.75A2-415[»]
5CPPX-ray2.08A2-415[»]
6CP4X-ray1.90A2-415[»]
6CPPX-ray1.90A2-415[»]
7CPPX-ray2.00A2-415[»]
8CPPX-ray2.10A2-415[»]
ProteinModelPortaliP00183.
SMRiP00183. Positions 10-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00183.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00359. BP450.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00183-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTETIQSNA NLAPLPPHVP EHLVFDFDMY NPSNLSAGVQ EAWAVLQESN
60 70 80 90 100
VPDLVWTRCN GGHWIATRGQ LIREAYEDYR HFSSECPFIP REAGEAYDFI
110 120 130 140 150
PTSMDPPEQR QFRALANQVV GMPVVDKLEN RIQELACSLI ESLRPQGQCN
160 170 180 190 200
FTEDYAEPFP IRIFMLLAGL PEEDIPHLKY LTDQMTRPDG SMTFAEAKEA
210 220 230 240 250
LYDYLIPIIE QRRQKPGTDA ISIVANGQVN GRPITSDEAK RMCGLLLVGG
260 270 280 290 300
LDTVVNFLSF SMEFLAKSPE HRQELIERPE RIPAACEELL RRFSLVADGR
310 320 330 340 350
ILTSDYEFHG VQLKKGDQIL LPQMLSGLDE RENACPMHVD FSRQKVSHTT
360 370 380 390 400
FGHGSHLCLG QHLARREIIV TLKEWLTRIP DFSIAPGAQI QHKSGIVSGV
410
QALPLVWDPA TTKAV
Length:415
Mass (Da):46,669
Last modified:January 23, 2007 - v2
Checksum:iE84641B4A65DD2D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 572Missing AA sequence (PubMed:7130171)Curated
Sequence conflicti277 – 2771E → Q AA sequence (PubMed:7130171)Curated
Sequence conflicti362 – 3621H → S AA sequence (PubMed:7130171)Curated
Sequence conflicti408 – 4081D → N AA sequence (PubMed:7130171)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12546 Genomic DNA. Translation: AAA25760.1.
D00528 Genomic DNA. Translation: BAA00412.1.
PIRiA25660. O4PSCP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12546 Genomic DNA. Translation: AAA25760.1 .
D00528 Genomic DNA. Translation: BAA00412.1 .
PIRi A25660. O4PSCP.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AKD X-ray 1.80 A 2-415 [» ]
1C8J X-ray 2.10 A/B 2-415 [» ]
1CP4 X-ray 1.90 A 2-415 [» ]
1DZ4 X-ray 1.60 A/B 2-415 [» ]
1DZ6 X-ray 1.90 A/B 2-415 [» ]
1DZ8 X-ray 1.90 A/B 2-415 [» ]
1DZ9 X-ray 1.90 A/B 2-415 [» ]
1GEB X-ray 2.03 A 1-415 [» ]
1GEK X-ray 1.70 A 1-415 [» ]
1GEM X-ray 2.00 A 1-415 [» ]
1GJM X-ray 2.20 A 2-415 [» ]
1IWI X-ray 2.00 A 1-415 [» ]
1IWJ X-ray 2.00 A 1-415 [» ]
1IWK X-ray 2.00 A 1-415 [» ]
1J51 X-ray 2.20 A/B/C/D 2-415 [» ]
1K2O X-ray 1.65 A/B 2-415 [» ]
1LWL X-ray 2.20 A 1-415 [» ]
1MPW X-ray 2.34 A/B 2-415 [» ]
1NOO X-ray 2.20 A 2-415 [» ]
1O76 X-ray 1.80 A/B 2-415 [» ]
1P2Y X-ray 2.30 A 2-415 [» ]
1P7R X-ray 2.85 A 2-415 [» ]
1PHA X-ray 1.63 A 2-415 [» ]
1PHB X-ray 1.60 A 2-415 [» ]
1PHC X-ray 1.60 A 2-415 [» ]
1PHD X-ray 1.60 A 2-415 [» ]
1PHE X-ray 1.60 A 2-415 [» ]
1PHF X-ray 1.60 A 2-415 [» ]
1PHG X-ray 1.60 A 2-415 [» ]
1QMQ X-ray 1.55 A 2-415 [» ]
1RE9 X-ray 1.45 A 2-415 [» ]
1RF9 X-ray 1.80 A 1-415 [» ]
1T85 X-ray 1.80 A 2-415 [» ]
1T86 X-ray 1.90 A/B 2-415 [» ]
1T87 X-ray 1.80 A/B 2-415 [» ]
1T88 X-ray 1.90 A/B 2-415 [» ]
1UYU X-ray 2.00 A/B 2-415 [» ]
1YRC X-ray 1.40 A 2-415 [» ]
1YRD X-ray 1.70 A 2-415 [» ]
2A1M X-ray 2.10 A/B 1-415 [» ]
2A1N X-ray 1.90 A/B 1-415 [» ]
2A1O X-ray 1.55 A/B 1-415 [» ]
2CP4 X-ray 2.10 A 2-415 [» ]
2CPP X-ray 1.63 A 2-415 [» ]
2FE6 X-ray 1.50 A 1-415 [» ]
2FER X-ray 1.70 A 11-415 [» ]
2FEU X-ray 1.70 A/B 11-415 [» ]
2FRZ X-ray 2.10 A/B 2-415 [» ]
2GQX X-ray 2.10 A/B 11-415 [» ]
2GR6 X-ray 2.30 A/B 11-415 [» ]
2H7Q X-ray 1.50 A 2-415 [» ]
2H7R X-ray 2.10 A 2-415 [» ]
2H7S X-ray 2.15 A/C 2-415 [» ]
2L8M NMR - A 1-415 [» ]
2LQD NMR - A 11-415 [» ]
2M56 NMR - A 12-415 [» ]
2QBL X-ray 1.80 A 1-415 [» ]
2QBM X-ray 1.80 A 1-415 [» ]
2QBN X-ray 1.75 A 1-415 [» ]
2QBO X-ray 1.90 A 1-415 [» ]
2Z97 X-ray 1.80 A 1-415 [» ]
2ZAW X-ray 1.55 A 1-415 [» ]
2ZAX X-ray 1.60 A 1-415 [» ]
2ZUH X-ray 1.55 A 1-415 [» ]
2ZUI X-ray 1.50 A 1-415 [» ]
2ZUJ X-ray 1.60 A 1-415 [» ]
2ZWT X-ray 1.35 A 1-415 [» ]
2ZWU X-ray 1.30 A 1-415 [» ]
3CP4 X-ray 2.30 A 2-415 [» ]
3CPP X-ray 1.90 A 2-415 [» ]
3FWF X-ray 1.83 A/B 11-415 [» ]
3FWG X-ray 1.55 A/B 11-415 [» ]
3FWI X-ray 2.40 A 11-415 [» ]
3FWJ X-ray 1.90 A 11-415 [» ]
3L61 X-ray 1.50 A 2-415 [» ]
3L62 X-ray 1.70 A 2-415 [» ]
3L63 X-ray 1.50 A 2-415 [» ]
3OIA X-ray 1.65 A 2-415 [» ]
3OL5 X-ray 1.75 A 2-415 [» ]
3P6M X-ray 2.00 A 2-415 [» ]
3P6N X-ray 1.70 A 2-415 [» ]
3P6O X-ray 2.00 A 2-415 [» ]
3P6P X-ray 1.90 A 2-415 [» ]
3P6Q X-ray 1.95 A 2-415 [» ]
3P6R X-ray 2.10 A 2-415 [» ]
3P6S X-ray 2.00 A 2-415 [» ]
3P6T X-ray 1.90 A 2-415 [» ]
3P6U X-ray 1.70 A 2-415 [» ]
3P6V X-ray 2.00 A 2-415 [» ]
3P6W X-ray 2.10 A 2-415 [» ]
3P6X X-ray 1.65 A 2-415 [» ]
3W9C X-ray 2.50 A 2-415 [» ]
4CP4 X-ray 2.10 A 2-415 [» ]
4CPP X-ray 2.11 A 2-415 [» ]
4EK1 X-ray 1.97 A/B 2-415 [» ]
4G3R X-ray 2.20 A/B 2-415 [» ]
4JWS X-ray 2.15 A/B 1-415 [» ]
4JWU X-ray 2.20 A/B 1-415 [» ]
4JX1 X-ray 2.09 A/B/E/F 1-415 [» ]
4KKY X-ray 2.00 X 2-414 [» ]
4L49 X-ray 2.13 A 1-415 [» ]
4L4A X-ray 2.10 A 1-415 [» ]
4L4B X-ray 2.10 A 1-415 [» ]
4L4C X-ray 2.20 A/B 1-415 [» ]
4L4D X-ray 2.10 A 1-415 [» ]
4L4E X-ray 1.26 A 1-415 [» ]
4L4F X-ray 1.29 A 1-415 [» ]
4L4G X-ray 1.55 A 1-415 [» ]
5CP4 X-ray 1.75 A 2-415 [» ]
5CPP X-ray 2.08 A 2-415 [» ]
6CP4 X-ray 1.90 A 2-415 [» ]
6CPP X-ray 1.90 A 2-415 [» ]
7CPP X-ray 2.00 A 2-415 [» ]
8CPP X-ray 2.10 A 2-415 [» ]
ProteinModelPortali P00183.
SMRi P00183. Positions 10-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29809N.

Chemistry

BindingDBi P00183.
ChEMBLi CHEMBL5594.
DrugBanki DB01011. Metyrapone.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00719 .
BioCyci MetaCyc:MONOMER-3021.

Miscellaneous databases

EvolutionaryTracei P00183.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00359. BP450.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli."
    Unger B.P., Gunsalus I.C., Sligar S.G.
    J. Biol. Chem. 261:1158-1163(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: G1 / ATCC 17453.
  2. "Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida."
    Koga H., Yamaguchi E., Matsunaga K., Aramaki H., Horiuchi T.
    J. Biochem. 106:831-836(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 386-415.
    Strain: G1 / ATCC 17453.
  3. "Amino acid sequence of the Pseudomonas putida cytochrome P-450. II. Cyanogen bromide peptides, acid cleavage peptides, and the complete sequence."
    Haniu M., Armes L.G., Yasunobu K.T., Shastry B.A., Gunsalus I.C.
    J. Biol. Chem. 257:12664-12671(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-415.
  4. "P-450 binding to substrates camphor and linalool versus pressure."
    Marden M.C., Hui Bon Hoa G.
    Arch. Biochem. Biophys. 253:100-107(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABSORPTION SPECTROSCOPY.
  5. "Dynamic behavior of the active site structure in bacterial cytochrome P-450."
    Jung C., Marlow F.
    Studia Biophys. 120:241-251(1987)
    Cited for: FOURIER-TRANSFORM INFRARED SPECTROSCOPY.
  6. "Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure."
    Hui Bon Hoa G., Di Primo C., Dondaine I., Sligar S.G., Gunsalus I.C., Douzou P.
    Biochemistry 28:651-656(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABSORPTION SPECTROSCOPY, FLUORESCENCE SPECTROSCOPY.
  7. "Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450."
    Nolting B., Jung C., Snatzke G.
    Biochim. Biophys. Acta 1100:171-176(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CIRCULAR DICHROISM ANALYSIS.
  8. "Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin."
    Deprez E., Gill E., Helms V., Wade R., Hui Bon Hoa G.
    J. Inorg. Biochem. 91:597-606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-PROTEIN INTERACTION.
  9. "The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450."
    Poulos T.L., Finzel B.C., Gunsalus I.C., Wagner G.C., Kraut J.
    J. Biol. Chem. 260:16122-16130(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  10. "Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer."
    Schlichting I., Jung C., Schulze H.
    FEBS Lett. 415:253-257(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  11. "Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein."
    Di Gleria K., Nickerson D.P., Hill H.A.O., Wong L.-L., Fueloep V.
    J. Am. Chem. Soc. 120:46-52(1998)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  12. "Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect."
    Vidakovic M., Sligar S.G., Li H., Poulos T.L.
    Biochemistry 37:9211-9219(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  13. "Optical detection of cytochrome P450 by sensitizer-linked substrates."
    Dmochowski I.J., Crane B.R., Wilker J.J., Winkler J.R., Gray H.B.
    Proc. Natl. Acad. Sci. U.S.A. 96:12987-12990(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  15. "X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center."
    Hishiki T., Shimada H., Nagano S., Egawa T., Kanamori Y., Makino R., Park S.-Y., Adachi S., Shiro Y., Ishimura Y.
    J. Biochem. 128:965-974(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
  16. "Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam."
    Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y.
    Biochemistry 40:2669-2677(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  17. "Probing the open state of cytochrome P450cam with ruthenium-linker substrates."
    Dunn A.R., Dmochowski I.J., Bilwes A.M., Gray H.B., Crane B.R.
    Proc. Natl. Acad. Sci. U.S.A. 98:12420-12425(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  18. "Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase -- structural models of the short-lived oxygen complexes."
    Fedorov R., Ghosh D.K., Schlichting I.
    Arch. Biochem. Biophys. 409:25-31(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  19. "1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton."
    Mouro C., Bondon A., Simmoneaux G., Jung C.
    FEBS Lett. 414:203-208(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCPXA_PSEPU
AccessioniPrimary (citable) accession number: P00183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3