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P14779

- CPXB_BACME

UniProt

P14779 - CPXB_BACME

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
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    FAD.
    FMN.
    Heme group.

    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

    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-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT     50
    RYLSSQRLIK EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA 100
    HNILLPSFSQ QAMKGYHAMM VDIAVQLVQK WERLNADEHI EVPEDMTRLT 150
    LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR ALDEAMNKLQ RANPDDPAYD 200
    ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN GKDPETGEPL 250
    DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV 300
    DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK 350
    GDELMVLIPQ LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA 400
    CIGQQFALHE ATLVLGMMLK HFDFEDHTNY ELDIKETLTL KPEGFVVKAK 450
    SKKIPLGGIP SPSTEQSAKK VRKKAENAHN TPLLVLYGSN MGTAEGTARD 500
    LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH PPDNAKQFVD 550
    WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD 600
    RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS 650
    AADMPLAKMH GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH 700
    LGVIPRNYEG IVNRVTARFG LDASQQIRLE AEEEKLAHLP LAKTVSVEEL 750
    LQYVELQDPV TRTQLRAMAA KTVCPPHKVE LEALLEKQAY KEQVLAKRLT 800
    MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE KQASITVSVV 850
    SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI 900
    MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL 950
    ENAQSEGIIT LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC 1000
    GDGSQMAPAV EATLMKSYAD VHQVSEADAR LWLQQLEEKG RYAKDVWAG 1049
    Length:1,049
    Mass (Da):117,781
    Last modified:January 23, 2007 - v2
    Checksum:iB0BE61F8A2EE33D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04832 Genomic DNA. Translation: AAA87602.1.
    PIRiA34286.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04832 Genomic DNA. Translation: AAA87602.1 .
    PIRi A34286.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 127 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