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1S7C

Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG12
AILE13
AHOH614
AHOH657

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AALA230
AARG232
AMES401
ATHR175
AHIS177
ASER207
ASER208
ATHR209

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ALYS132
AGLY133
AALA134
APHE136
AASP137

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
APRO128
AMET129
ALYS217

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
ATHR252
ATYR253
AGLU254
AHOH681
AHOH685
AHOH704

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 401
ChainResidue
ASER149
ACYS150
ATHR151
AHIS177
ATHR209
AGLY210
ASO4502
AHOH688
AHOH703

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA148-LEU155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:10978154
ChainResidueDetails
ATHR151

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984, ECO:0000269|Ref.18
ChainResidueDetails
AILE13

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984
ChainResidueDetails
ALEU35
AGLU315

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219
ChainResidueDetails
AASP79

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219
ChainResidueDetails
AGLY121

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154
ChainResidueDetails
ACYS150
AGLY210

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
AALA181

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154
ChainResidueDetails
AVAL233

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073
ChainResidueDetails
AALA178

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS116
AASP125
AALA214
AVAL218
ALEU226
AALA250
AALA258
AALA262

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
AGLY133
AASP193
ALYS331

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ATYR139

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
AHIS177
ACYS150

223166

PDB entries from 2024-07-31

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