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2DY3

Crystal Structure of alanine racemase from Corynebacterium glutamicum

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
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0006522biological_processalanine metabolic process
B0008784molecular_functionalanine racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0030632biological_processD-alanine biosynthetic process
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0006522biological_processalanine metabolic process
C0008784molecular_functionalanine racemase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016853molecular_functionisomerase activity
C0030170molecular_functionpyridoxal phosphate binding
C0030632biological_processD-alanine biosynthetic process
D0003824molecular_functioncatalytic activity
D0005829cellular_componentcytosol
D0006522biological_processalanine metabolic process
D0008784molecular_functionalanine racemase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0016853molecular_functionisomerase activity
D0030170molecular_functionpyridoxal phosphate binding
D0030632biological_processD-alanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 401
ChainResidue
AVAL32
ALEU217
ATYR346
BASP305
BHOH567
ALYS34
ATYR38
ATRP80
AHIS158
AASN198
ASER199
AARG214
AGLY216

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 401
ChainResidue
AHOH556
BVAL32
BLYS34
BTYR38
BTRP80
BHIS158
BASN198
BSER199
BARG214
BPRO215
BGLY216
BLEU217
BTYR346

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP C 401
ChainResidue
CVAL32
CLYS34
CTYR38
CTRP80
CHIS158
CASN198
CSER199
CPRO200
CARG214
CPRO215
CGLY216
CLEU217
CTYR346
CHOH535

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP D 401
ChainResidue
CHOH536
DVAL32
DLYS34
DTYR38
DTRP80
DHIS158
DASN198
DSER199
DARG214
DPRO215
DGLY216
DLEU217
DTYR346
DHOH463

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
ALYS34
BLYS34
CLYS34
DLYS34

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
ATYR256
BTYR256
CTYR256
DTYR256

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
AARG129
AMET304
BARG129
BMET304
CARG129
CMET304
DARG129
DMET304

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS34
BLYS34
CLYS34
DLYS34

218853

PDB entries from 2024-04-24

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