Structure of PDB 6yck Chain A

Receptor sequence
>6yckA (length=403) Species: 385957 (Amycolatopsis sp. ATCC 39116) [Search protein sequence]
ERPDLAWLDEVTMTQLERNPYEVYERLRAEAPLAFVPVLGSYVASTAEVC
REVATSPDFEAVITPAGGRTFGHPAIIGVNGDIHADLRSMVEPALQPAEV
DRWIDDLVRPIARRYLERFENDGHAELVAQYCEPVSVRSLGDLLGLQEVD
SDKLREWFAKLNRSFTNAAVDENGEFANPEGFAEGDQAKAEIRAVVDPLI
DKWIEHPDDSAISHWLHDGMPPGQTRDREYIYPTIYVYLLGAMQEPGHGM
ASTLVGLFSRPEQLEEVVDDPTLIPRAIAEGLRWTSPIWSAAARISTKPV
TIAGVDLPAGTPVMLSYGSANHDTGKYEAPSQYDLHRPPLPHLAFGAGNH
ACAGIYFANHVMRIALEELFEAIPNLERDTREGVEFWGWGFRGPTSLHVT
WEV
3D structure
PDB6yck Engineering a Cytochrome P450 for Demethylation of Lignin-Derived Aromatic Aldehydes.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R167 Q248 E249 C356 A357 G358
Catalytic site (residue number reindexed from 1) R163 Q244 E245 C352 A353 G354
Enzyme Commision number 1.14.14.-
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 A I81 H88 R92 Y242 A246 E249 P250 I292 R298 Y321 A348 F349 G350 H354 C356 F361 A362 M366 I77 H84 R88 Y238 A242 E245 P246 I288 R294 Y317 A344 F345 G346 H350 C352 F357 A358 M362
BS02 V55 A F169 V241 G245 A296 F165 V237 G241 A292
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6yck, PDBe:6yck, PDBj:6yck
PDBsum6yck
PubMed34467290
UniProtP0DPQ7|GCOA_AMYS7 Aromatic O-demethylase, cytochrome P450 subunit (Gene Name=gcoA)

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