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5HRC

Crystal structure of an aspartate/glutamate racemase in complex with L-aspartate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0036361molecular_functionracemase activity, acting on amino acids and derivatives
A0047661molecular_functionamino-acid racemase activity
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0036361molecular_functionracemase activity, acting on amino acids and derivatives
B0047661molecular_functionamino-acid racemase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue ASP A 301
ChainResidue
AMET10
AGLU199
AGLN52
ATHR83
AASN84
ATHR85
ATHR125
APHE162
ACYS197
ATHR198

site_idAC2
Number of Residues13
Detailsbinding site for residue NHE A 302
ChainResidue
AHIS41
AGLU66
AALA67
AGLY70
AARG73
AGLU172
AHOH454
AHOH525
AHOH553
AHOH556
AHOH562
BALA74
BHOH489

site_idAC3
Number of Residues9
Detailsbinding site for residue ASP B 301
ChainResidue
BMET10
BGLN52
BTHR83
BASN84
BTHR85
BCYS197
BTHR198
BGLU199
BHOH436

Functional Information from PROSITE/UniProt
site_idPS00923
Number of Residues10
DetailsASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. IVlCtNTMHK
ChainResidueDetails
AILE79-LYS88

site_idPS00924
Number of Residues11
DetailsASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. VIfGCTEIGlL
ChainResidueDetails
AVAL193-LEU203

223532

PDB entries from 2024-08-07

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