Structure of PDB 1b74 Chain A

Receptor sequence
>1b74A (length=252) Species: 2714 (Aquifex pyrophilus) [Search protein sequence]
MKIGIFDSGVGGLTVLKAIRNRYRKVDIVYLGDTARVPYGIRSKDTIIRY
SLECAGFLKDKGVDIIVVACNTASAYALERLKKEINVPVFGVIEPGVKEA
LKKSRNKKIGVIGTPATVKSGAYQRKLEEGGADVFAKACPLFAPLAEEGL
LEGEITRKVVEHYLKEFKGKIDTLILGCTHYPLLKKEIKKFLGDAEVVDS
SEALSLSLHNFIKDDGSSSLELFFTDLSPNLQFLIKLILGRDYPVKLAEG
VF
3D structure
PDB1b74 Structure and mechanism of glutamate racemase from Aquifex pyrophilus.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D7 S8 C70 T72 T114 E147 C178 H180
Catalytic site (residue number reindexed from 1) D7 S8 C70 T72 T114 E147 C178 H180
Enzyme Commision number 5.1.1.3: glutamate racemase.
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 DGN A C70 N71 G177 C178 C70 N71 G177 C178 MOAD: Ki=50mM
PDBbind-CN: -logKd/Ki=1.30,Ki=50mM
Gene Ontology
Molecular Function
GO:0008881 glutamate racemase activity
GO:0016853 isomerase activity
GO:0016855 racemase and epimerase activity, acting on amino acids and derivatives
GO:0036361 racemase activity, acting on amino acids and derivatives
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1b74, PDBe:1b74, PDBj:1b74
PDBsum1b74
PubMed10331867
UniProtP56868|MURI_AQUPY Glutamate racemase (Gene Name=murI)

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