Structure of PDB 6g5q Chain A

Receptor sequence
>6g5qA (length=374) Species: 63186 (Zobellia galactanivorans) [Search protein sequence]
KKSELPDPFEKARESKGYGEMNDQDDPVTMLLRHKDVRKSAHNYKTFQSG
AVPGRIVIPSEVDIRDTRQIPFEVDPPVHGVYRAIVEPWFKRPLQAEYQE
KLTAQISEIVEETLLKGSVEVVTDFALRLQSRALTLLLNTPFSESETWIS
WGTDGDKANILYHYIDEQIDRASENPGDDMYSVLLNSEFEGRKLTKEEVK
GVMVLTFAGGRDTVINAVTNSIAYLAEHPEALERLRKEPEITGRAVEEMI
RYFSPLTQMGRVVTEDTHVCEHAVKADSRISLCWASANRDAAVFENPNEI
VLDRKVNPHVGFGFSHHNCLGATHARQILKILLQTLAQKVASFEILDYKE
NIEDLDHFQRKVGFHNIQIKFNPL
3D structure
PDB6g5q Specificity and mechanism of carbohydrate demethylation by cytochrome P450 monooxygenases.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D223 T224 C330 L331 G332
Catalytic site (residue number reindexed from 1) D212 T213 C319 L320 G321
Enzyme Commision number 1.14.15.-
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 EMZ A E62 Q70 F73 L216 A219 E61 Q69 F72 L205 A208 MOAD: Kd=0.98mM
BS02 HEM A F73 H80 R84 L216 T217 G220 G221 T224 L267 R272 G322 F323 H328 C330 G332 F72 H79 R83 L205 T206 G209 G210 T213 L256 R261 G311 F312 H317 C319 G321
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:6g5q, PDBe:6g5q, PDBj:6g5q
PDBsum6g5q
PubMed30404923
UniProtG0L713

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