Structure of PDB 8dme Chain B

Receptor sequence

>8dmeB (length=1034) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581)

KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFFGDGLFTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENK
RQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDE
NIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPV
PSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDE
LMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIG
QQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKK
IPLKKVRKKAENAHNTPLLVLYGSNMGTAEGTARDLADIAMSKGFAPQVA
TLDSHAGNLPREGAVLIVTASYNGHPPDNAKQFVDWLDQASADEVKGVRY
SVFGCGDKNWATTYQKVPAFIDETLAAKGAENIADRGEADASDDFEGTYE
EWREHMWSDVAAYFNLDIENSEDNKSTLSLQFVDSAADMPLAKMHGAFST
NVVASKELQQPGSARSTRHLEIELPKEASYQEGDHLGVIPRNYEGIVNRV
TARFGLDASQQIRLEAEEEKLAHLPLAKTVSVEELLQYVELQDPVTRTQL
RAMAAKTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPACEMKF
SEFIALLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIA
SNYLAELQEGDTITCFISTPQSEFTLPKDPETPLIMVGPGTGVAPFRGFV
QARKQLKEQGQSLGEAHLYFGCRSPHEDYLYQEELENAQSEGIITLHTAF
SRMPNQPKTYVQHVMEQDGKKLIELLDQGAHFYICGDGSQMAPAVEATLM
KSYADVHQVSEADARLWLQQLEEKGRYAKDVWAG

3D structure

• PDB: 8dme Insight into the conformational dynamics of cytochrome P450 CYP102A1 enzyme using Cryo-EM
• Chain: B
• Resolution: 6.5 Å

Enzymatic activity

• Enzyme Commision number: 1.14.14.1: unspecific monooxygenase.
  1.6.2.4: NADPH--hemoprotein reductase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	HEM	B	K69 L86 F87 W96 F107 F261 A264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406	K67 L84 F85 W94 F105 F259 A262 G263 T266 F329 P390 F391 R396 C398 I399 G400 A404
BS02	1C6	B	F87 L188 A328 P329 L437	F85 L186 A326 P327 L435
BS03	FMN	B	S488 N489 M490 G491 T492 A493 A534 S535 Y536 N537 G570 D571 W574 T577 Y578	S474 N475 M476 G477 T478 A479 A520 S521 Y522 N523 G556 D557 W560 T563 Y564
BS04	FAD	B	H699 R797 R827 Y828 Y829 S830 T845 V846 E852 A853 W854 Y860 G862 I863 A864 S865 T905 W1046 G1048	H685 R783 R813 Y814 Y815 S816 T831 V832 E838 A839 W840 Y846 G848 I849 A850 S851 T891 W1032 G1034

Gene Ontology

Molecular Function

• GO:0003958 NADPH-hemoprotein reductase activity
• GO:0004497 monooxygenase activity
• GO:0005506 iron ion binding
• GO:0010181 FMN binding
• GO:0016491 oxidoreductase activity
• GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
• GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
• GO:0020037 heme binding
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding
• GO:0050660 flavin adenine dinucleotide binding
• GO:0070330 aromatase activity

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:8dme, PDBe:8dme, PDBj:8dme
• PDBsum: 8dme
• UniProt: P14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)