Structure of PDB 1mty Chain D

Receptor sequence
>1mtyD (length=512) Species: 243233 (Methylococcus capsulatus str. Bath) [Search protein sequence]
AANRAPTSVNAQEVHRWLQSFNWDFKNNRTKYATKYKMANETKEQFKLIA
KEYARMEAVKDERQFGSLQVALTRLNAGVRVHPKWNETMKVVSNFLEVGE
YNAIAATGMLWDSAQAAEQKNGYLAQVLDEIRHTHQCAYVNYYFAKNGQD
PAGHNDARRTRTIGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTN
PLIVAVTEWAAANGDEITPTVFLSIETDELRHMANGYQTVVSIANDPASA
KYLNTDLNNAFWTQQKYFTPVLGMLFEYGSKFKVEPWVKTWDRWVYEDWG
GIWIGRLGKYGVESPRSLKDAKQDAYWAHHDLYLLAYALWPTGFFRLALP
DQEEMEWFEANYPGWYDHYGKIYEEWRARGCEDPSSGFIPLMWFIENNHP
IYIDRVSQVPFCPSLAKGASTLRVHEYNGEMHTFSDQWGERMWLAEPERY
ECQNIFEQYEGRELSEVIAELHGLRSDGKTLIAQPHVRGDKLWTLDDIKR
LNCVFKNPVKAF
3D structure
PDB1mty Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions.
ChainD
Resolution1.7 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) E100 E130 H133 E195 E229 H232
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 FE D E144 E209 E243 H246 E130 E195 E229 H232
BS02 FE D E114 E144 H147 E100 E130 H133
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:1mty, PDBe:1mty, PDBj:1mty
PDBsum1mty
PubMed9329079
UniProtP22869|MEMA_METCA Methane monooxygenase component A alpha chain (Gene Name=mmoX)

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