Structure of PDB 4m0x Chain A

Receptor sequence
>4m0xA (length=369) Species: 37919 (Rhodococcus opacus) [Search protein sequence]
TTITEMSATIVDLPSRRPHKFAATTMHHQSIVLVRVRDSDGGEGIGEAVT
PGGPWWGGESVETIKTIIDQYLAPVIIGRDPSTIGVASQSMDGLVFGNSV
AKAAIETALWDDRERRSRIPVSDLLGGLRRKRIPITWAFSAGSASDLIDE
AAQKLDVGHRSFKFKMGAEPADTDSRRVLDVLECIPDECAVIVDPNGRWS
ELEAHRWLPILADAGVTVAEQPIARWNTDGLARLRDKLSIPIMADESVTT
VQQAIALADAGAVSAFAIKIPKSGGLSRAREIAAIAEASGLACFGAATPE
SSVMGAISAQLYGTMPDLSVGCELFGPGLLIDEVVTEPLKYDRGELLIPT
GPGSGVNLDEERLRKYSRD
3D structure
PDB4m0x Structural basis for the substrate specificity and the absence of dehalogenation activity in 2-chloromuconate cycloisomerase from Rhodococcus opacus 1CP.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T52 G55 A140 K165 K167 D196 N198 E222 D247 E248 S249 A269 K271 A298 A299 T300 C324 E325 L326
Catalytic site (residue number reindexed from 1) T50 G53 A138 K163 K165 D194 N196 E220 D245 E246 S247 A267 K269 A296 A297 T298 C322 E323 L324
Enzyme Commision number ?
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 MN A D196 E222 D247 D194 E220 D245
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0018849 muconate cycloisomerase activity
GO:0018850 chloromuconate cycloisomerase activity
GO:0030145 manganese ion 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:4m0x, PDBe:4m0x, PDBj:4m0x
PDBsum4m0x
PubMed24768773
UniProtQ8G9L1

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