Structure of PDB 1rky Chain A Binding Site BS05

Receptor Information
>1rky Chain A (length=735) Species: 4922 (Komagataella pastoris) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AECVSNENVEIEAPKTNIWTSLAKEEVQEVLDLLHSTYNITEVTKADFFS
NYVLWIETLKPNKTEALTYLDEDGDLPPRNARTVVYFGEGEEGYFEELKV
GPLPVSDETTIEPLSFYNTNGKSKLPFEVGHLDRIKSAAKSSFLNKNLNT
TIMRDVLEGLIGVPYEDMGCHSAAPQLHDPATGATVDYGTCNINTENDAE
NLVPTGFFFKFDMTGRDVSQWKMLEYIYNNKVYTSAEELYEAMQKDDFVT
LPKIDVDNLDWTVIQRNDSAPVRHLDDRKSPRLVEPEGRRWAYDGDEEYF
SWMDWGFYTSWSRDTGISFYDITFKGERIVYELSLQELIAEYGSDDPFNQ
HTFYSDISYGVGNRFSLVPGYDCPSTAGYFTTDTFEYDEFYNRTLSYCVF
ENQEDYSLLRHTGASYSAITQNPTLNVRFISTIGNYDYNFLYKFFLDGTL
EVSVRAAGYIQAGYWNPETSAPYGLKIHDVLSGSFHDHVLNYKVDLDVGG
TKNRASQYVMKDVDVEYPWAPGTVYNTKQIAREVFENEDFNGINWPENGQ
GILLIESAEETNSFGNPRAYNIMPGGGGVHRIVKNSRSGPETQNWARSNL
FLTKHKDTELRSSTALNTNALYDPPVNFNAFLDDESLDGEDIVAWVNLGL
HHLPNSNDLPNTIFSTAHASFMLTPFNYFDSENSRDTTQQVFYTYDDETE
ESNWEFYGNDWSSCGVEVAEPNFEDYTYGRGTRIN
Ligand information
Ligand IDXE
InChIInChI=1S/Xe
InChIKeyFHNFHKCVQCLJFQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Xe]
FormulaXe
NameXENON
ChEMBLCHEMBL1236802
DrugBankDB13453
ZINC
PDB chain1rky Chain A Residue 902 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1rky Using Xenon as a Probe for Dioxygen-binding Sites in Copper Amine Oxidases
Resolution1.68 Å
Binding residue
(original residue number in PDB)		M265 L266 E267 Y268 T276 S277
Binding residue
(residue number reindexed from 1)		M223 L224 E225 Y226 T234 S235
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y384 D398 Y478 H528 H530 H694
Catalytic site (residue number reindexed from 1) Y342 D356 Y436 H486 H488 H652
Enzyme Commision number 1.4.3.-
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0048038 quinone binding
GO:0052597 diamine oxidase activity
Biological Process
GO:0009308 amine metabolic process
Cellular Component
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rky, PDBe:1rky, PDBj:1rky
PDBsum1rky
PubMed15533431
UniProtQ96X16

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