Structure of PDB 2jfz Chain B

Receptor sequence
>2jfzB (length=248) Species: 210 (Helicobacter pylori) [Search protein sequence]
MKIGVFDSGVGGFSVLKSLLKARLFDEIIYYGDSARVPYGTKDPTTIKQF
GLEALDFFKPHEIELLIVACNTASALALEEMQKYSKIPIVGVIEPSILAI
KRQVEDKNAPILVLGTKATIQSNAYDNALKQQGYLNISHLATSLFVPLIE
ESILEGELLETCMHYYFTPLEILPEVIILGCTHFPLIAQKIEGYFMGHFA
LPTPPLLIHSGDAIVEYLQQKYALPKVEFHASGDVIWLERQAKEWLKL
3D structure
PDB2jfz Exploitation of Structural and Regulatory Diversity in Glutamate Racemases
ChainB
Resolution1.86 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 E150 C181 H183
Catalytic site (residue number reindexed from 1) D7 S8 C70 E150 C181 H183
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 003 B V10 G11 K17 I149 S152 H183 L186 Q248 W252 V10 G11 K17 I149 S152 H183 L186 Q241 W245 MOAD: Ki=5.8uM
BS02 DGL B S8 P38 Y39 G40 C70 N71 T72 C181 T182 H183 S8 P38 Y39 G40 C70 N71 T72 C181 T182 H183
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
GO:0042802 identical protein binding
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization

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Molecular Function
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Biological Process
External links
PDB RCSB:2jfz, PDBe:2jfz, PDBj:2jfz
PDBsum2jfz
PubMed17568739
UniProtQ9ZLT0|MURI_HELPJ Glutamate racemase (Gene Name=murI)

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