2EP7
Structural study of Project ID aq_1065 from Aquifex aeolicus VF5
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 | 0005737 | cellular_component | cytoplasm |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| 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 | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | GLY9 |
| A | ALA96 |
| A | THR97 |
| A | GLY98 |
| A | PHE100 |
| A | THR120 |
| A | ALA121 |
| A | CYS152 |
| A | THR182 |
| A | ASN183 |
| A | LEU190 |
| A | GLY11 |
| A | ASN322 |
| A | HOH410 |
| A | HOH419 |
| A | HOH425 |
| A | HOH428 |
| A | HOH434 |
| A | HOH450 |
| A | HOH524 |
| A | HOH526 |
| A | HOH527 |
| A | ARG12 |
| A | ILE13 |
| A | ASN33 |
| A | ASP34 |
| A | LEU35 |
| A | GLN77 |
| A | LYS78 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 402 |
| Chain | Residue |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN33 |
| B | ASP34 |
| B | LEU35 |
| B | GLN77 |
| B | LYS78 |
| B | ALA96 |
| B | THR97 |
| B | GLY98 |
| B | PHE100 |
| B | THR120 |
| B | CYS152 |
| B | THR182 |
| B | ASN183 |
| B | LEU190 |
| B | PRO191 |
| B | ASN322 |
| B | HOH403 |
| B | HOH406 |
| B | HOH415 |
| B | HOH426 |
| B | HOH431 |
| B | HOH432 |
| B | HOH454 |
| B | HOH513 |
| B | HOH514 |
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 | ALA150-LEU157 |
| site_id | PS00430 |
| Number of Residues | 70 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. maikvgingfgrigrsffraswgreeieivaindltdakhlahllkydsvhgifkgsveakd.....................................................DSIVVDGK |
| Chain | Residue | Details |
| A | MET1-LYS70 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2007","submissionDatabase":"PDB data bank","title":"Structural study of Project ID aq_1065 from Aquifex aeolicus VF5.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]} |
| 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 | HIS179 | |
| A | CYS152 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | HIS179 | |
| B | CYS152 |
