Structure of PDB 2efu Chain A

Receptor sequence
>2efuA (length=362) Species: 529 (Brucella anthropi) [Search protein sequence]
SDLNNAIQGILDDHVARGVVGVSLALCLPGEETSLYQSGYADKFNKMPMT
GDHLFRIASCTKSFIATGLHLLVQDGTVDLDEPITRWFPDLPKAAQMPVR
ILLNHRSGLPDFETSMPMISDKSWTAQEIVDFSFRHGVQKEPWHGMEYSN
TGYVLAGMIIAHETGKPYSDHLRSRIFAPLGMKDTWVGTHETFPIEREAR
GYMHAAADDENPQWDVSGAGDPVDGVWDSTEWFPLSGANAAGDMVSTPRD
IVKFLNALFDGRILDQKRLWEMKDNIKPAFFPGSNTVANGHGLLLMRYGS
SELKGHLGQIPGHTSIMGRDEETGAALMLIQNSGAGDFESFYLKGVNEPV
DRVLEAIKNSRS
3D structure
PDB2efu Structures of D-amino-acid amidase complexed with L-phenylalanine and with L-phenylalanine amide: insight into the D-stereospecificity of D-amino-acid amidase from Ochrobactrum anthropi SV3.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S60 K63 D112 E114 I120 Y149 S150 V155 S218 G313
Catalytic site (residue number reindexed from 1) S59 K62 D111 E113 I119 Y148 S149 V154 S217 G312
Enzyme Commision number ?
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 PHE A S60 E114 Y149 F234 A239 G309 Q310 S59 E113 Y148 F233 A238 G308 Q309
Gene Ontology
Molecular Function
GO:0008233 peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2efu, PDBe:2efu, PDBj:2efu
PDBsum2efu
PubMed18323628
UniProtQ9LCC8

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