Structure of PDB 2jfz Chain A

Receptor sequence

>2jfzA (length=255) Species: 210 (Helicobacter pylori)

MKIGVFDSGVGGFSVLKSLLKARLFDEIIYYGDSARVPYGTKDPTTIKQF
GLEALDFFKPHEIELLIVACNTASALALEEMQKYSKIPIVGVIEPSILAI
KRQVEDKNAPILVLGTKATIQSNAYDNALKQQGYLNISHLATSLFVPLIE
ESILEGELLETCMHYYFTPLEILPEVIILGCTHFPLIAQKIEGYFMGHFA
LPTPPLLIHSGDAIVEYLQQKYALKNNACTFPKVEFHASGDVIWLERQAK
EWLKL

3D structure

• PDB: 2jfz Exploitation of Structural and Regulatory Diversity in Glutamate Racemases
• Chain: A
• Resolution: 1.86 Å

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	A	V10 G11 F13 S152 H183 L186 Q248 W252	V10 G11 F13 S152 H183 L186 Q248 W252	MOAD: Ki=5.8uM PDBbind-CN: -logKd/Ki=5.24,Ki=5.8uM
BS02	DGL	A	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

External links

• PDB: RCSB:2jfz, PDBe:2jfz, PDBj:2jfz
• PDBsum: 2jfz
• PubMed: 17568739
• UniProt: Q9ZLT0|MURI_HELPJ Glutamate racemase (Gene Name=murI)