Structure of PDB 3uj2 Chain G

Receptor sequence
>3uj2G (length=423) Species: 411490 (Anaerostipes caccae L1-92) [Search protein sequence]
NYLEIEKVIGREIIDSRGNPTVEAEVYLAGGVTGRGTAPSGGEFEALELR
DGDKGRFGGKGVTKAVQNINTEISEILSGMDASDIYAVDRAMIDADGTKD
KSKFGANAVLAVSIACAKAAAAALGVPLYRFLGGLNANRLPVPMMNILNG
GAHAANTVDVQEFMIMPVGAESFREALRQCTEVFHALAGLLKSKGLATSV
GDEGGFAPDLASDEEAIEYILEAVKLAGYEPGRDFVLAMDAASSEWKGEK
KGEYILPKCKRKFASEELVAHWKSLCERYPIVSIEDGLDEEDWEGWQYMT
RELGDKIQLVGDDLFVTNTERLNKGIKERCGNSILIKLNQIGTVSETLEA
IKMAHKAGYTAVVSHRSGETEDTTIADLAVALNTGQIKTGAPSRSERVAK
YNQLLRIEEELGDSAVYPGFTTF
3D structure
PDB3uj2 CRYSTAL STRUCTURE OF AN ENOLASE FROM ANAEROSTIPES CACCAE (EFI TARGET EFI-502054) WITH BOUND MG AND SULFATE
ChainG
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H157 E166 E207 D244 E289 D316 K341 H369 K392
Catalytic site (residue number reindexed from 1) H153 E162 E203 D240 E285 D312 K337 H365 K388
Enzyme Commision number 4.2.1.11: phosphopyruvate hydratase.
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 MG G D244 E289 D316 D240 E285 D312
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004634 phosphopyruvate hydratase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
Cellular Component
GO:0000015 phosphopyruvate hydratase complex
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0009986 cell surface

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Molecular Function
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Cellular Component
External links
PDB RCSB:3uj2, PDBe:3uj2, PDBj:3uj2
PDBsum3uj2
PubMed
UniProtB0MAG5

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