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6DLI

Crystal structure of glutamate racemase from Thermus thermophilus in complex with Beta-chloro-D-alanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0008360biological_processregulation of cell shape
A0008881molecular_functionglutamate racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016853molecular_functionisomerase activity
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0047661molecular_functionamino-acid racemase activity
A0071555biological_processcell wall organization
B0008360biological_processregulation of cell shape
B0008881molecular_functionglutamate racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016853molecular_functionisomerase activity
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0047661molecular_functionamino-acid racemase activity
B0071555biological_processcell wall organization
C0008360biological_processregulation of cell shape
C0008881molecular_functionglutamate racemase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016853molecular_functionisomerase activity
C0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
C0047661molecular_functionamino-acid racemase activity
C0071555biological_processcell wall organization
D0008360biological_processregulation of cell shape
D0008881molecular_functionglutamate racemase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0016853molecular_functionisomerase activity
D0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
D0047661molecular_functionamino-acid racemase activity
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue C2N A 301
ChainResidue
AASP12
ASER13
ACYS75
AASN76
ATHR77
ATHR116
ACYS176
ATHR177

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 302
ChainResidue
ATYR128
AASP130
AARG106

site_idAC3
Number of Residues9
Detailsbinding site for residue C2N B 301
ChainResidue
BASP12
BSER13
BTYR44
BCYS75
BASN76
BTHR77
BTHR116
BCYS176
BTHR177

site_idAC4
Number of Residues10
Detailsbinding site for residue C2N C 301
ChainResidue
CASP12
CSER13
CPRO43
CTYR44
CGLY45
CCYS75
CASN76
CTHR77
CTHR116
CTHR177

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL C 302
ChainResidue
CVAL68
CVAL92

site_idAC6
Number of Residues8
Detailsbinding site for residue C2N D 301
ChainResidue
DASP12
DSER13
DCYS75
DASN76
DTHR77
DTHR116
DCYS176
DTHR177

site_idAC7
Number of Residues2
Detailsbinding site for residue GOL D 302
ChainResidue
DVAL68
DVAL92

Functional Information from PROSITE/UniProt
site_idPS00923
Number of Residues9
DetailsASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. VVaC.NTASS
ChainResidueDetails
AVAL72-SER80

site_idPS00924
Number of Residues11
DetailsASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. LIlGCTHYPfL
ChainResidueDetails
ALEU172-LEU182

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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