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6KMA

Crystal structure of SucA with glycolaldehyde-1-13C from Vibrio vulnificus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A0030976molecular_functionthiamine pyrophosphate binding
A0045252cellular_componentoxoglutarate dehydrogenase complex
A0046872molecular_functionmetal ion binding
B0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase activity
B0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
B0030976molecular_functionthiamine pyrophosphate binding
B0045252cellular_componentoxoglutarate dehydrogenase complex
B0046872molecular_functionmetal ion binding
C0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
C0005829cellular_componentcytosol
C0006099biological_processtricarboxylic acid cycle
C0016491molecular_functionoxidoreductase activity
C0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
C0030976molecular_functionthiamine pyrophosphate binding
C0045252cellular_componentoxoglutarate dehydrogenase complex
C0046872molecular_functionmetal ion binding
D0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
D0005829cellular_componentcytosol
D0006099biological_processtricarboxylic acid cycle
D0016491molecular_functionoxidoreductase activity
D0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
D0030976molecular_functionthiamine pyrophosphate binding
D0045252cellular_componentoxoglutarate dehydrogenase complex
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue P6G A 1001
ChainResidue
APHE304
ASER305
ALEU319
AALA320
APHE321
AVAL332
ASER336
AMET529
AARG713

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 1002
ChainResidue
AGLU665
AHOH1164
BGLU665
BHOH1138
BHOH1164
BHOH1202

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 1003
ChainResidue
AASP360
AASN393
AVAL395
ATPP1004
AHOH1113

site_idAC4
Number of Residues23
Detailsbinding site for residue TPP A 1004
ChainResidue
AHIS263
AARG264
ASER324
AHIS325
ALEU326
AGLY359
AASP360
ASER361
AALA362
AGLN366
AASN393
AVAL395
AHIS463
AMG1003
AHOH1113
AHOH1173
AHOH1257
BGLN619
BLEU662
BGLU664
BGLN688
BPHE692
BDW31001

site_idAC5
Number of Residues5
Detailsbinding site for residue DW3 A 1005
ChainResidue
ATYR300
AHIS301
ASER324
AHOH1235
BDW31001

site_idAC6
Number of Residues7
Detailsbinding site for residue DW3 A 1006
ChainResidue
AGLN688
APHE689
APHE692
AHIS732
BPHE397
BTPP1004
BDW31005

site_idAC7
Number of Residues7
Detailsbinding site for residue DW3 B 1001
ChainResidue
APHE397
ATPP1004
ADW31005
BGLN688
BPHE689
BPHE692
BHIS732

site_idAC8
Number of Residues9
Detailsbinding site for residue P6G B 1002
ChainResidue
BPHE304
BSER305
BLEU319
BALA320
BPHE321
BVAL332
BSER336
BARG713
BHOH1133

site_idAC9
Number of Residues5
Detailsbinding site for residue MG B 1003
ChainResidue
BASP360
BASN393
BVAL395
BTPP1004
BHOH1117

site_idAD1
Number of Residues24
Detailsbinding site for residue TPP B 1004
ChainResidue
BHOH1362
AGLN619
ALEU662
AGLU664
AGLN688
APHE692
ADW31006
BHIS263
BARG264
BSER324
BHIS325
BLEU326
BGLY359
BASP360
BSER361
BALA362
BGLN366
BASN393
BVAL395
BHIS463
BMG1003
BHOH1117
BHOH1193
BHOH1319

site_idAD2
Number of Residues6
Detailsbinding site for residue DW3 B 1005
ChainResidue
AHIS732
ADW31006
BTYR300
BHIS301
BSER324
BHOH1188

site_idAD3
Number of Residues8
Detailsbinding site for residue P6G C 1001
ChainResidue
CSER305
CALA318
CLEU319
CPHE321
CVAL332
CSER336
CARG713
CHOH1148

site_idAD4
Number of Residues6
Detailsbinding site for residue CA C 1002
ChainResidue
CGLU665
CHOH1131
CHOH1180
CHOH1191
DGLU665
DHOH1124

site_idAD5
Number of Residues5
Detailsbinding site for residue MG C 1003
ChainResidue
CASP360
CASN393
CVAL395
CTPP1004
CHOH1165

site_idAD6
Number of Residues24
Detailsbinding site for residue TPP C 1004
ChainResidue
CHIS263
CARG264
CSER324
CHIS325
CLEU326
CGLY359
CASP360
CSER361
CALA362
CGLN366
CASN393
CVAL395
CGLY396
CHIS463
CMG1003
CHOH1165
CHOH1171
CHOH1197
DGLN619
DLEU662
DGLU664
DGLN688
DPHE692
DDW31001

site_idAD7
Number of Residues6
Detailsbinding site for residue DW3 C 1005
ChainResidue
CTYR300
CHIS301
CSER324
CHOH1294
DHIS732
DDW31001

site_idAD8
Number of Residues6
Detailsbinding site for residue DW3 C 1006
ChainResidue
CPHE692
CHIS732
CHOH1211
DHIS463
DTPP1004
DDW31005

site_idAD9
Number of Residues6
Detailsbinding site for residue DW3 D 1001
ChainResidue
CTPP1004
CDW31005
DPHE689
DPHE692
DHIS732
DHOH1186

site_idAE1
Number of Residues7
Detailsbinding site for residue P6G D 1002
ChainResidue
DSER305
DLEU319
DALA320
DVAL332
DSER336
DARG713
DHOH1160

site_idAE2
Number of Residues5
Detailsbinding site for residue MG D 1003
ChainResidue
DASP360
DASN393
DVAL395
DTPP1004
DHOH1142

site_idAE3
Number of Residues25
Detailsbinding site for residue TPP D 1004
ChainResidue
CGLN619
CLEU662
CGLU664
CGLN688
CPHE692
CDW31006
DHIS263
DARG264
DSER324
DHIS325
DLEU326
DGLY359
DASP360
DSER361
DALA362
DGLN366
DASN393
DVAL395
DGLY396
DHIS463
DMG1003
DHOH1142
DHOH1169
DHOH1207
DHOH1332

site_idAE4
Number of Residues6
Detailsbinding site for residue DW3 D 1005
ChainResidue
CDW31006
DHIS263
DTYR300
DHIS301
DSER324
DHOH1301

221051

PDB entries from 2024-06-12

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