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3HUR

Crystal structure of alanine racemase from Oenococcus oeni

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006522biological_processalanine metabolic process
A0008784molecular_functionalanine racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0030632biological_processD-alanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 395
ChainResidue
AASN204
ASER205
AGLY225
AGLN226
AHOH410

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 396
ChainResidue
AARG368
AASP291
AGLY292
ATRP293
APRO367

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 397
ChainResidue
AARG7
AALA40
AASP41
AASN67
AGLU70
ALYS370

Functional Information from PROSITE/UniProt
site_idPS00395
Number of Residues11
DetailsALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVlKADGYGLG
ChainResidueDetails
AALA36-GLY46

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ALYS39
AARG134

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ATHR316
ATYR270

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PDB entries from 2024-07-24

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