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3E5P

Crystal structure of alanine racemase from E.faecalis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006522biological_processalanine metabolic process
A0008784molecular_functionalanine racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016020cellular_componentmembrane
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0030632biological_processD-alanine biosynthetic process
A0046677biological_processresponse to antibiotic
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006522biological_processalanine metabolic process
B0008784molecular_functionalanine racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016020cellular_componentmembrane
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0030632biological_processD-alanine biosynthetic process
B0046677biological_processresponse to antibiotic
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006522biological_processalanine metabolic process
C0008784molecular_functionalanine racemase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016020cellular_componentmembrane
C0016853molecular_functionisomerase activity
C0030170molecular_functionpyridoxal phosphate binding
C0030632biological_processD-alanine biosynthetic process
C0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLP A 390
ChainResidue
ALYS40
AHOH431
ATYR44
AHIS169
AASN206
ASER207
AARG222
AGLY224
AVAL225
ATYR356

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PPI A 400
ChainResidue
ATYR267
ATYR286
ACYS313
AMET314
CTYR356

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPE A 430
ChainResidue
AARG292
AHIS293
AGLN295
AARG311
ALYS350
CGLU352
CTHR353
C2PE401

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP B 390
ChainResidue
BLYS40
BTYR44
BARG139
BHIS169
BASN206
BSER207
BARG222
BGLY224
BVAL225
BTYR356
BHOH402
BHOH403

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PPI B 400
ChainResidue
BTYR267
BTYR286
BILE354
BTYR356
BHOH422

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 2PE C 401
ChainResidue
AHIS293
ALYS350
ALEU351
AGLU352
AILE354
AEPE430
CARG292
CHIS293
CGLN295
CARG311
CLYS350
CGLU352

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP C 390
ChainResidue
CVAL38
CLYS40
CTYR44
CLEU86
CHIS169
CASN206
CSER207
CARG222
CGLY224
CVAL225
CTYR356
CHOH425

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PPI C 400
ChainResidue
CTYR267
CTYR286
CCYS313
CMET314

Functional Information from PROSITE/UniProt
site_idPS00395
Number of Residues11
DetailsALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANGYGHG
ChainResidueDetails
AALA37-GLY47

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ALYS40
AARG139

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
BLYS40
BARG139

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
CLYS40
CARG139

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
ACYS313
ATYR267

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
BCYS313
BTYR267

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bd0
ChainResidueDetails
CCYS313
CTYR267

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PDB entries from 2025-07-02

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