Structure of PDB 2vvt Chain A

Receptor sequence
>2vvtA (length=269) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
VPRGSHMSNQEAIGLIDSGVGGLTVLKEALKQLPNERLIYLGDTARCPYG
PRPAEQVVQFTWEMADFLLKKRIKMLVIACNTATAVALEEIKAALPIPVV
GVILPGARAAVKVTKNNKIGVIGTLGTIKSASYEIAIKSKAPAIEVTSLA
CPKFVPIVESNQYRSSVAKKIVAETLQALQLKGLDTLILGCTHYPLLRPV
IQNVMGSHVTLIDSGAETVGEVSMLLDYFDIAHTPPHEFYTTGSAKMFEE
IASSWLGIENLKAQQIHLG
3D structure
PDB2vvt Exploring 9-Benzyl Purines as Inhibitors of Glutamate Racemase (Muri) in Gram-Positive Bacteria.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D11 S12 C74 E153 C185 H187
Catalytic site (residue number reindexed from 1) D17 S18 C80 E159 C191 H193
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 A V14 V152 E153 N155 H187 L190 I250 W254 V20 V158 E159 N161 H193 L196 I251 W255 MOAD: ic50=5.8uM
PDBbind-CN: -logKd/Ki=5.24,IC50=5.8uM
BindingDB: IC50=5800nM
BS02 DGL A S12 P42 Y43 G44 C74 N75 T76 C185 T186 H187 S18 P48 Y49 G50 C80 N81 T82 C191 T192 H193
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2vvt, PDBe:2vvt, PDBj:2vvt
PDBsum2vvt
PubMed18614367
UniProtQ836J0|MURI_ENTFA Glutamate racemase (Gene Name=murI)

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