Structure of PDB 1fyz Chain A

Receptor sequence
>1fyzA (length=511) Species: 414 (Methylococcus capsulatus) [Search protein sequence]
NRAPTSVNAQEVHRWLQSFNWDFKNNRTKYATKYKMANETKEQFKLIAKE
YARMEAVKDERQFGSLQDALTRLNAGVRVHPKWNETMKVVSNFLEVGEYN
AIAATGMLWDSAQAAEQKNGYLAQVLDEIRHTHQCAYVNYYFAKNGQDPA
GHNDARRTRTIGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPL
IVAVTEWAAANGDEITPTVFLSIETDELRHMANGYQTVVSIANDPASAKY
LNTDLNNAFWTQQKYFTPVLGMLFEYGSKFKVEPWVKTWDRWVYEDWGGI
WIGRLGKYGVESPRSLKDAKQDAYWAHHDLYLLAYALWPTGFFRLALPDQ
EEMEWFEANYPGWYDHYGKIYEEWRARGCEDPSSGFIPLMWFIENNHPIY
IDRVSQVPFCPSLAKGASTLRVHEYNGEMHTFSDQWGERMWLAEPERYEC
QNIFEQYEGRELSEVIAELHGLRSDGKTLIAQPHVRGDKLWTLDDIKRLN
CVFKNPVKAFN
3D structure
PDB1fyz Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E114 E144 H147 E209 E243 H246
Catalytic site (residue number reindexed from 1) E98 E128 H131 E193 E227 H230
Enzyme Commision number 1.14.13.25: methane monooxygenase (soluble).
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 FE2 A E114 E144 H147 E243 E98 E128 H131 E227
BS02 FE2 A Q140 E144 E209 E243 H246 Q124 E128 E193 E227 H230
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005515 protein binding
GO:0015049 methane monooxygenase [NAD(P)H] activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006730 one-carbon metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1fyz, PDBe:1fyz, PDBj:1fyz
PDBsum1fyz
PubMed11456616
UniProtP22869|MEMA_METCA Methane monooxygenase component A alpha chain (Gene Name=mmoX)

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