Structure of PDB 2vvt Chain B

Receptor sequence

>2vvtB (length=266) Species: 1351 (Enterococcus faecalis)

NQEAIGLIDSGVGGLTVLKEALKQLPNERLIYLGDTARCPYGPRPAEQVV
QFTWEMADFLLKKRIKMLVIACNTATAVALEEIKAALPIPVVGVILPGAR
AAVKVTKNNKIGVIGTLGTIKSASYEIAIKSKAPAIEVTSLACPKFVPIV
ESNQYRSSVAKKIVAETLQALQLKGLDTLILGCTHYPLLRPVIQNVMGSH
VTLIDSGAETVGEVSMLLDYFDIAHTPEAPTQPHEFYTTGSAKMFEEIAS
SWLGIENLKAQQIHLG

3D structure

• PDB: 2vvt Exploring 9-Benzyl Purines as Inhibitors of Glutamate Racemase (Muri) in Gram-Positive Bacteria.
• Chain: B
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D11 S12 C74 E153 C185 H187
• Catalytic site (residue number reindexed from 1): D9 S10 C72 E151 C183 H185
• 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	I24	B	V152 E153 N155 E249 I250 W254	V150 E151 N153 E247 I248 W252	MOAD: ic50=5.8uM BindingDB: IC50=5800nM
BS02	DGL	B	S12 P42 Y43 G44 C74 N75 T76 C185 T186 H187	S10 P40 Y41 G42 C72 N73 T74 C183 T184 H185

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:2vvt, PDBe:2vvt, PDBj:2vvt
• PDBsum: 2vvt
• PubMed: 18614367
• UniProt: Q836J0|MURI_ENTFA Glutamate racemase (Gene Name=murI)