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5W16

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0008881molecular_functionglutamate racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0047661molecular_functionamino-acid racemase activity
B0008881molecular_functionglutamate racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0047661molecular_functionamino-acid racemase activity
C0008881molecular_functionglutamate racemase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
C0047661molecular_functionamino-acid racemase activity
D0008881molecular_functionglutamate racemase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
D0047661molecular_functionamino-acid racemase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue DGL A 301
ChainResidue
AASP12
ACYS176
ATHR177
AHOH428
AHOH461
ASER13
APRO43
ATYR44
AGLY45
ACYS75
AASN76
ATHR77
ATHR116

site_idAC2
Number of Residues8
Detailsbinding site for residue NO3 A 302
ChainResidue
AGLY14
AVAL15
ATHR39
AVAL42
ALEU238
AHOH443
AHOH482
AHOH519

site_idAC3
Number of Residues8
Detailsbinding site for residue NO3 A 303
ChainResidue
AALA40
AARG41
ALYS47
AHOH468
AHOH528
BALA40
BARG41
BLYS47

site_idAC4
Number of Residues5
Detailsbinding site for residue NO3 A 304
ChainResidue
APRO48
AALA50
AMET51
AARG54
BARG251

site_idAC5
Number of Residues5
Detailsbinding site for residue NO3 A 305
ChainResidue
ALEU195
ALEU196
AASP197
AGLU200
AHOH525

site_idAC6
Number of Residues3
Detailsbinding site for residue NO3 A 306
ChainResidue
AARG106
AVAL129
AASP130

site_idAC7
Number of Residues1
Detailsbinding site for residue CL A 307
ChainResidue
AGLN117

site_idAC8
Number of Residues14
Detailsbinding site for residue DGL B 301
ChainResidue
BASP12
BSER13
BPRO43
BTYR44
BGLY45
BCYS75
BASN76
BTHR77
BTHR116
BCYS176
BTHR177
BHOH421
BHOH431
BHOH454

site_idAC9
Number of Residues9
Detailsbinding site for residue NO3 B 302
ChainResidue
BGLY14
BVAL15
BTHR39
BVAL42
BTYR235
BLEU238
BHOH420
BHOH467
BHOH511

site_idAD1
Number of Residues6
Detailsbinding site for residue NO3 B 303
ChainResidue
AARG251
BPRO48
BALA50
BMET51
BARG54
BHOH404

site_idAD2
Number of Residues3
Detailsbinding site for residue CL B 304
ChainResidue
BTHR116
BGLN117
BHOH559

site_idAD3
Number of Residues1
Detailsbinding site for residue CL B 305
ChainResidue
BTHR224

site_idAD4
Number of Residues14
Detailsbinding site for residue DGL C 301
ChainResidue
CASP12
CSER13
CPRO43
CTYR44
CGLY45
CCYS75
CASN76
CTHR77
CTHR116
CCYS176
CTHR177
CHOH407
CHOH417
CHOH424

site_idAD5
Number of Residues8
Detailsbinding site for residue NO3 C 302
ChainResidue
CALA40
CARG41
CLYS47
CHOH507
DALA40
DARG41
DLYS47
DHOH455

site_idAD6
Number of Residues7
Detailsbinding site for residue NO3 C 303
ChainResidue
AARG221
CGLN66
CPHE225
CLEU227
CARG250
CHOH420
AARG30

site_idAD7
Number of Residues9
Detailsbinding site for residue NO3 C 304
ChainResidue
CGLY14
CVAL15
CTHR39
CVAL42
CLEU238
CHOH444
CHOH448
CHOH506
CHOH518

site_idAD8
Number of Residues5
Detailsbinding site for residue NO3 C 305
ChainResidue
CPRO48
CALA50
CMET51
CARG54
DARG251

site_idAD9
Number of Residues4
Detailsbinding site for residue NO3 C 306
ChainResidue
CALA87
CGLU88
CHOH478
CHOH524

site_idAE1
Number of Residues3
Detailsbinding site for residue CL C 307
ChainResidue
CTHR116
CGLN117
CHOH563

site_idAE2
Number of Residues1
Detailsbinding site for residue CL C 308
ChainResidue
CVAL153

site_idAE3
Number of Residues2
Detailsbinding site for residue CL C 309
ChainResidue
CASP130
CHOH502

site_idAE4
Number of Residues14
Detailsbinding site for residue DGL D 301
ChainResidue
DASP12
DSER13
DPRO43
DTYR44
DGLY45
DCYS75
DASN76
DTHR77
DTHR116
DCYS176
DTHR177
DHOH420
DHOH423
DHOH454

site_idAE5
Number of Residues7
Detailsbinding site for residue NO3 D 302
ChainResidue
BARG30
BGLU219
BARG221
DPHE225
DLEU227
DARG250
DHOH445

site_idAE6
Number of Residues9
Detailsbinding site for residue NO3 D 303
ChainResidue
DGLY14
DVAL15
DTHR39
DVAL42
DLEU238
DHOH432
DHOH487
DHOH528
DHOH537

site_idAE7
Number of Residues5
Detailsbinding site for residue NO3 D 304
ChainResidue
CARG251
DPRO48
DALA50
DMET51
DARG54

site_idAE8
Number of Residues5
Detailsbinding site for residue NO3 D 305
ChainResidue
DARG106
DVAL129
DASP130
DHOH418
DHOH529

site_idAE9
Number of Residues3
Detailsbinding site for residue CL D 306
ChainResidue
DTHR116
DGLN117
DHOH558

site_idAF1
Number of Residues1
Detailsbinding site for residue CL D 307
ChainResidue
DARG54

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

251174

PDB entries from 2026-03-25

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