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P14779

- CPXB_BACME

UniProt

P14779 - CPXB_BACME

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Protein

Bifunctional P-450/NADPH-P450 reductase

Gene

cyp102A1

Organism
Bacillus megaterium
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi401 – 4011Iron (heme axial ligand)

GO - Molecular functioni

  1. aromatase activity Source: UniProtKB-EC
  2. FMN binding Source: InterPro
  3. heme binding Source: InterPro
  4. identical protein binding Source: IntAct
  5. iron ion binding Source: InterPro
  6. NADPH-hemoprotein reductase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17698.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional P-450/NADPH-P450 reductase
Alternative name(s):
Cytochrome P450(BM-3)
Short name:
Cytochrome P450BM-3
Including the following 2 domains:
Cytochrome P450 102 (EC:1.14.14.1)
NADPH--cytochrome P450 reductase (EC:1.6.2.4)
Gene namesi
Name:cyp102A1
Synonyms:cyp102
OrganismiBacillus megaterium
Taxonomic identifieri1404 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 10491048Bifunctional P-450/NADPH-P450 reductasePRO_0000052205Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7701704,EBI-7701704

Protein-protein interaction databases

MINTiMINT-8313368.

Structurei

Secondary structure

1
1049
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 153Combined sources
Helixi18 – 214Combined sources
Helixi26 – 3712Combined sources
Beta strandi39 – 457Combined sources
Beta strandi48 – 536Combined sources
Helixi56 – 627Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 703Combined sources
Helixi74 – 8310Combined sources
Helixi87 – 893Combined sources
Beta strandi92 – 943Combined sources
Helixi95 – 10410Combined sources
Helixi105 – 1084Combined sources
Turni110 – 1123Combined sources
Helixi113 – 13220Combined sources
Helixi142 – 15918Combined sources
Helixi165 – 1673Combined sources
Helixi173 – 18715Combined sources
Helixi188 – 1903Combined sources
Helixi197 – 1993Combined sources
Helixi200 – 22728Combined sources
Helixi234 – 2407Combined sources
Turni244 – 2463Combined sources
Helixi252 – 28332Combined sources
Helixi285 – 29814Combined sources
Beta strandi301 – 3033Combined sources
Helixi306 – 3105Combined sources
Helixi313 – 32513Combined sources
Beta strandi331 – 3388Combined sources
Beta strandi340 – 3423Combined sources
Turni343 – 3453Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi353 – 3575Combined sources
Helixi358 – 3614Combined sources
Helixi365 – 3684Combined sources
Turni370 – 3734Combined sources
Helixi377 – 3804Combined sources
Helixi383 – 3853Combined sources
Helixi397 – 3993Combined sources
Helixi404 – 42118Combined sources
Beta strandi422 – 4254Combined sources
Beta strandi434 – 4429Combined sources
Beta strandi446 – 4516Combined sources
Beta strandi483 – 4886Combined sources
Beta strandi490 – 4923Combined sources
Helixi493 – 50614Combined sources
Turni507 – 5093Combined sources
Beta strandi513 – 5164Combined sources
Helixi517 – 5193Combined sources
Beta strandi526 – 5349Combined sources
Turni543 – 5453Combined sources
Helixi546 – 5538Combined sources
Beta strandi565 – 5717Combined sources
Helixi576 – 5783Combined sources
Helixi581 – 59111Combined sources
Turni592 – 5943Combined sources
Beta strandi599 – 6057Combined sources
Helixi610 – 62819Combined sources
Beta strandi663 – 67210Combined sources
Beta strandi682 – 6887Combined sources
Beta strandi700 – 7034Combined sources
Helixi709 – 71911Combined sources
Beta strandi726 – 7294Combined sources
Beta strandi741 – 7466Combined sources
Helixi747 – 7504Combined sources
Helixi751 – 7533Combined sources
Beta strandi756 – 7594Combined sources
Helixi762 – 7709Combined sources
Helixi775 – 7839Combined sources
Helixi787 – 7937Combined sources
Turni794 – 7985Combined sources
Helixi801 – 8077Combined sources
Helixi815 – 8206Combined sources
Beta strandi828 – 8314Combined sources
Turni836 – 8383Combined sources
Beta strandi842 – 8487Combined sources
Beta strandi851 – 8533Combined sources
Beta strandi857 – 8626Combined sources
Helixi864 – 8718Combined sources
Beta strandi877 – 8837Combined sources
Beta strandi899 – 9024Combined sources
Helixi905 – 9084Combined sources
Helixi909 – 92315Combined sources
Beta strandi931 – 9388Combined sources
Turni940 – 9423Combined sources
Helixi947 – 9559Combined sources
Beta strandi960 – 9678Combined sources
Helixi976 – 9827Combined sources
Helixi984 – 9929Combined sources
Beta strandi996 – 10027Combined sources
Turni1003 – 10053Combined sources
Helixi1006 – 102217Combined sources
Helixi1026 – 103813Combined sources
Beta strandi1042 – 10476Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BU7X-ray1.65A/B2-456[»]
1BVYX-ray2.03A/B2-459[»]
F460-650[»]
1FAGX-ray2.70A/B/C/D2-472[»]
1FAHX-ray2.30A/B2-472[»]
1JMEX-ray2.00A/B2-456[»]
1JPZX-ray1.65A/B2-471[»]
1P0VX-ray2.05A/B2-456[»]
1P0WX-ray2.00A/B2-456[»]
1P0XX-ray2.00A/B2-456[»]
1SMIX-ray2.00A/B2-472[»]
1SMJX-ray2.75A/B/C/D2-472[»]
1YQOX-ray1.90A/B2-456[»]
1YQPX-ray1.80A/B2-456[»]
1ZO4X-ray1.46A/B2-471[»]
1ZO9X-ray1.70A/B2-471[»]
1ZOAX-ray1.74A/B2-471[»]
2BMHX-ray2.00A/B2-456[»]
2HPDX-ray2.00A/B2-472[»]
2IJ2X-ray1.20A/B2-471[»]
2IJ3X-ray1.90A/B2-471[»]
2IJ4X-ray2.40A/B2-471[»]
2J1MX-ray1.70A/B2-456[»]
2J4SX-ray2.10A/B2-456[»]
2NNBX-ray1.90A/B2-472[»]
2UWHX-ray2.80A/B/C/D/E/F2-459[»]
2X7YX-ray2.10A/B2-456[»]
2X80X-ray2.30A/B2-456[»]
3BENX-ray1.65A/B1-470[»]
3CBDX-ray2.65A/B2-456[»]
3DGIX-ray1.95A/B2-456[»]
3EKBX-ray2.30A/B2-471[»]
3EKDX-ray2.50A/B2-471[»]
3EKFX-ray2.10A/B2-471[»]
3HF2X-ray2.20A/B1-482[»]
3KX3X-ray1.80A/B2-471[»]
3KX4X-ray1.95A/B2-471[»]
3KX5X-ray1.69A/B2-471[»]
3M4VX-ray1.90A/B1-482[»]
3NPLX-ray2.40A/B1-464[»]
3PSXX-ray1.90A/B1-482[»]
4DQKX-ray2.40A/B659-1049[»]
4DQLX-ray2.15A/B657-1049[»]
4DTWX-ray1.80A/B2-464[»]
4DTYX-ray1.45A/B2-464[»]
4DTZX-ray1.55A/B2-464[»]
4DU2X-ray1.90A/B1-464[»]
4DUAX-ray2.00A/B2-464[»]
4DUBX-ray1.70A/B1-464[»]
4DUCX-ray1.92A/B1-464[»]
4DUDX-ray1.85A/B2-464[»]
4DUEX-ray1.70A/B2-464[»]
4DUFX-ray1.80A/B/C/D2-464[»]
4H23X-ray3.30A/B1-464[»]
4H24X-ray2.50A/B/C/D1-464[»]
4HGFX-ray1.70A/B2-456[»]
4HGGX-ray1.70A/B2-456[»]
4HGHX-ray1.40A/B2-456[»]
4HGIX-ray1.50A/B2-456[»]
4HGJX-ray1.90A/B2-456[»]
4KEWX-ray1.89A/B2-456[»]
4KEYX-ray2.05A/B2-456[»]
4KF0X-ray1.45A/B2-458[»]
4KF2X-ray1.82A/B2-458[»]
4KPAX-ray2.00A1-471[»]
4KPBX-ray2.10A/B1-471[»]
4O4PX-ray1.83A/B2-456[»]
ProteinModelPortaliP14779.
SMRiP14779. Positions 2-459, 480-631.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14779.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini483 – 622140Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini660 – 892233FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 472471Cytochrome P450Add
BLAST
Regioni473 – 1049577NADPH-P-450 reductaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the cytochrome P450 family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR023206. Bifunctional_P450_P450_red.
IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00067. p450. 1 hit.
[Graphical view]
PIRSFiPIRSF000209. Bifunctional_P450_P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF48264. SSF48264. 1 hit.
SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14779-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT
60 70 80 90 100
RYLSSQRLIK EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA
110 120 130 140 150
HNILLPSFSQ QAMKGYHAMM VDIAVQLVQK WERLNADEHI EVPEDMTRLT
160 170 180 190 200
LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR ALDEAMNKLQ RANPDDPAYD
210 220 230 240 250
ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN GKDPETGEPL
260 270 280 290 300
DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV
310 320 330 340 350
DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK
360 370 380 390 400
GDELMVLIPQ LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA
410 420 430 440 450
CIGQQFALHE ATLVLGMMLK HFDFEDHTNY ELDIKETLTL KPEGFVVKAK
460 470 480 490 500
SKKIPLGGIP SPSTEQSAKK VRKKAENAHN TPLLVLYGSN MGTAEGTARD
510 520 530 540 550
LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH PPDNAKQFVD
560 570 580 590 600
WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD
610 620 630 640 650
RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS
660 670 680 690 700
AADMPLAKMH GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH
710 720 730 740 750
LGVIPRNYEG IVNRVTARFG LDASQQIRLE AEEEKLAHLP LAKTVSVEEL
760 770 780 790 800
LQYVELQDPV TRTQLRAMAA KTVCPPHKVE LEALLEKQAY KEQVLAKRLT
810 820 830 840 850
MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE KQASITVSVV
860 870 880 890 900
SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI
910 920 930 940 950
MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL
960 970 980 990 1000
ENAQSEGIIT LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC
1010 1020 1030 1040
GDGSQMAPAV EATLMKSYAD VHQVSEADAR LWLQQLEEKG RYAKDVWAG
Length:1,049
Mass (Da):117,781
Last modified:January 23, 2007 - v2
Checksum:iB0BE61F8A2EE33D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04832 Genomic DNA. Translation: AAA87602.1.
PIRiA34286.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04832 Genomic DNA. Translation: AAA87602.1 .
PIRi A34286.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BU7 X-ray 1.65 A/B 2-456 [» ]
1BVY X-ray 2.03 A/B 2-459 [» ]
F 460-650 [» ]
1FAG X-ray 2.70 A/B/C/D 2-472 [» ]
1FAH X-ray 2.30 A/B 2-472 [» ]
1JME X-ray 2.00 A/B 2-456 [» ]
1JPZ X-ray 1.65 A/B 2-471 [» ]
1P0V X-ray 2.05 A/B 2-456 [» ]
1P0W X-ray 2.00 A/B 2-456 [» ]
1P0X X-ray 2.00 A/B 2-456 [» ]
1SMI X-ray 2.00 A/B 2-472 [» ]
1SMJ X-ray 2.75 A/B/C/D 2-472 [» ]
1YQO X-ray 1.90 A/B 2-456 [» ]
1YQP X-ray 1.80 A/B 2-456 [» ]
1ZO4 X-ray 1.46 A/B 2-471 [» ]
1ZO9 X-ray 1.70 A/B 2-471 [» ]
1ZOA X-ray 1.74 A/B 2-471 [» ]
2BMH X-ray 2.00 A/B 2-456 [» ]
2HPD X-ray 2.00 A/B 2-472 [» ]
2IJ2 X-ray 1.20 A/B 2-471 [» ]
2IJ3 X-ray 1.90 A/B 2-471 [» ]
2IJ4 X-ray 2.40 A/B 2-471 [» ]
2J1M X-ray 1.70 A/B 2-456 [» ]
2J4S X-ray 2.10 A/B 2-456 [» ]
2NNB X-ray 1.90 A/B 2-472 [» ]
2UWH X-ray 2.80 A/B/C/D/E/F 2-459 [» ]
2X7Y X-ray 2.10 A/B 2-456 [» ]
2X80 X-ray 2.30 A/B 2-456 [» ]
3BEN X-ray 1.65 A/B 1-470 [» ]
3CBD X-ray 2.65 A/B 2-456 [» ]
3DGI X-ray 1.95 A/B 2-456 [» ]
3EKB X-ray 2.30 A/B 2-471 [» ]
3EKD X-ray 2.50 A/B 2-471 [» ]
3EKF X-ray 2.10 A/B 2-471 [» ]
3HF2 X-ray 2.20 A/B 1-482 [» ]
3KX3 X-ray 1.80 A/B 2-471 [» ]
3KX4 X-ray 1.95 A/B 2-471 [» ]
3KX5 X-ray 1.69 A/B 2-471 [» ]
3M4V X-ray 1.90 A/B 1-482 [» ]
3NPL X-ray 2.40 A/B 1-464 [» ]
3PSX X-ray 1.90 A/B 1-482 [» ]
4DQK X-ray 2.40 A/B 659-1049 [» ]
4DQL X-ray 2.15 A/B 657-1049 [» ]
4DTW X-ray 1.80 A/B 2-464 [» ]
4DTY X-ray 1.45 A/B 2-464 [» ]
4DTZ X-ray 1.55 A/B 2-464 [» ]
4DU2 X-ray 1.90 A/B 1-464 [» ]
4DUA X-ray 2.00 A/B 2-464 [» ]
4DUB X-ray 1.70 A/B 1-464 [» ]
4DUC X-ray 1.92 A/B 1-464 [» ]
4DUD X-ray 1.85 A/B 2-464 [» ]
4DUE X-ray 1.70 A/B 2-464 [» ]
4DUF X-ray 1.80 A/B/C/D 2-464 [» ]
4H23 X-ray 3.30 A/B 1-464 [» ]
4H24 X-ray 2.50 A/B/C/D 1-464 [» ]
4HGF X-ray 1.70 A/B 2-456 [» ]
4HGG X-ray 1.70 A/B 2-456 [» ]
4HGH X-ray 1.40 A/B 2-456 [» ]
4HGI X-ray 1.50 A/B 2-456 [» ]
4HGJ X-ray 1.90 A/B 2-456 [» ]
4KEW X-ray 1.89 A/B 2-456 [» ]
4KEY X-ray 2.05 A/B 2-456 [» ]
4KF0 X-ray 1.45 A/B 2-458 [» ]
4KF2 X-ray 1.82 A/B 2-458 [» ]
4KPA X-ray 2.00 A 1-471 [» ]
4KPB X-ray 2.10 A/B 1-471 [» ]
4O4P X-ray 1.83 A/B 2-456 [» ]
ProteinModelPortali P14779.
SMRi P14779. Positions 2-459, 480-631.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-8313368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17698.

Miscellaneous databases

EvolutionaryTracei P14779.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi IPR023206. Bifunctional_P450_P450_red.
IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00067. p450. 1 hit.
[Graphical view ]
PIRSFi PIRSF000209. Bifunctional_P450_P450R. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF48264. SSF48264. 1 hit.
SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Coding nucleotide, 5' regulatory, and deduced amino acid sequences of P-450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from Bacillus megaterium."
    Ruettinger R.T., Wen L.-P., Fulco A.J.
    J. Biol. Chem. 264:10987-10995(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Fatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions."
    Boddupalli S.S., Pramanik B.C., Slaughter C.A., Estabrook R.W., Peterson J.A.
    Arch. Biochem. Biophys. 292:20-28(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  3. "Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's."
    Ravichandran K.G., Boddupalli S.S., Hasemann C.A., Peterson J.A., Deisenhofer J.
    Science 261:731-736(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-472.
  4. "The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid."
    Li H.Y., Poulos T.L.
    Nat. Struct. Biol. 4:140-146(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-472.
  5. "Structure of a cytochrome P450-redox partner electron-transfer complex."
    Sevrioukova I.F., Li H., Zhang H., Peterson J.A., Poulos T.L.
    Proc. Natl. Acad. Sci. U.S.A. 96:1863-1868(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-650.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471.

Entry informationi

Entry nameiCPXB_BACME
AccessioniPrimary (citable) accession number: P14779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 129 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, Multifunctional enzyme

Documents

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

External Data

Dasty 3