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6IO6

Silver-bound Glyceraldehyde-3-phosphate dehydrogenase A at non-catalytic site

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 AG A 401
ChainResidue
AGLU287
ACYS289
AAG402
AHOH501

site_idAC2
Number of Residues4
Detailsbinding site for residue AG A 402
ChainResidue
AGLU287
ACYS289
AAG401
AHOH502

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
ACYS150

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
AARG12

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984
ChainResidueDetails
AASP34
AASN314

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219
ChainResidueDetails
AARG78

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219
ChainResidueDetails
ATHR120

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10978154
ChainResidueDetails
ASER149
ATHR209

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
ATHR180

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154
ChainResidueDetails
AARG232

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073
ChainResidueDetails
AHIS177

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS115
ALYS124
ALYS213
ALYS217
ALYS225
ALYS249
ALYS257
ALYS261

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS132
ALYS192
ALYS331

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS138

227111

PDB entries from 2024-11-06

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