1S7C
Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006006 | biological_process | glucose metabolic process |
A | 0006096 | biological_process | glycolytic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0042802 | molecular_function | identical protein binding |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
A | 0072524 | biological_process | pyridine-containing compound metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | ARG12 |
A | ILE13 |
A | HOH614 |
A | HOH657 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | ALA230 |
A | ARG232 |
A | MES401 |
A | THR175 |
A | HIS177 |
A | SER207 |
A | SER208 |
A | THR209 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | LYS132 |
A | GLY133 |
A | ALA134 |
A | PHE136 |
A | ASP137 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | PRO128 |
A | MET129 |
A | LYS217 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | THR252 |
A | TYR253 |
A | GLU254 |
A | HOH681 |
A | HOH685 |
A | HOH704 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MES A 401 |
Chain | Residue |
A | SER149 |
A | CYS150 |
A | THR151 |
A | HIS177 |
A | THR209 |
A | GLY210 |
A | SO4502 |
A | HOH688 |
A | HOH703 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
A | ALA148-LEU155 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636984","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli.","authors":["Shin D.H.","Thor J.","Yokota H.","Kim R.","Kim S.H."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636984","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli.","authors":["Shin D.H.","Thor J.","Yokota H.","Kim R.","Kim S.H."]}},{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"2659073","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
A | HIS177 | |
A | CYS150 |