Structure of PDB 3out Chain C

Receptor sequence
>3outC (length=264) Species: 119856 (Francisella tularensis subsp. tularensis) [Search protein sequence]
LDNRPIGVFDSGIGGLTIVKNLMSILPNEDIIYFGDIARIPYGTKSRATI
QKFAAQTAKFLIDQEVKAIIIACNTISAIAKDIVQEIAKAIPVIDVITAG
VSLVDNLNTVGVIATPATINSNAYALQIHKKNPNIEVYSNPCGLFVSMIE
EGFVSGHIVELVAKEYLSYFHDKNIQALILGCTHYPIIKESIAKILDVKL
IDPSLQASKMLYSLLFENKLLNTTKSNPEYRFYVTDIPLKFRSVGEMFLQ
TEMQHLEIVSLDSY
3D structure
PDB3out Crystal structure of glutamate racemase from Francisella tularensis subsp. tularensis SCHU S4 in complex with D-glutamate.
ChainC
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 E151 C183 H185
Catalytic site (residue number reindexed from 1) D10 S11 C73 E150 C182 H184
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 DGL C S12 P42 Y43 G44 C74 N75 T76 C183 T184 S11 P41 Y42 G43 C73 N74 T75 C182 T183
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
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Biological Process
External links
PDB RCSB:3out, PDBe:3out, PDBj:3out
PDBsum3out
PubMed
UniProtQ5NFN6

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