3L6O
Crystal Structure of Phosphate bound apo Glyceraldehyde-3-phosphate dehydrogenase 1 from MRSA252 at 2.2 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| O | 0000166 | molecular_function | nucleotide binding |
| O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| O | 0005737 | cellular_component | cytoplasm |
| O | 0006006 | biological_process | glucose metabolic process |
| O | 0006096 | biological_process | glycolytic process |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| O | 0050661 | molecular_function | NADP binding |
| O | 0051287 | molecular_function | NAD binding |
| P | 0000166 | molecular_function | nucleotide binding |
| P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| P | 0005737 | cellular_component | cytoplasm |
| P | 0006006 | biological_process | glucose metabolic process |
| P | 0006096 | biological_process | glycolytic process |
| P | 0016491 | molecular_function | oxidoreductase activity |
| P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| P | 0050661 | molecular_function | NADP binding |
| P | 0051287 | molecular_function | NAD binding |
| Q | 0000166 | molecular_function | nucleotide binding |
| Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0006006 | biological_process | glucose metabolic process |
| Q | 0006096 | biological_process | glycolytic process |
| Q | 0016491 | molecular_function | oxidoreductase activity |
| Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| Q | 0050661 | molecular_function | NADP binding |
| Q | 0051287 | molecular_function | NAD binding |
| R | 0000166 | molecular_function | nucleotide binding |
| R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| R | 0005737 | cellular_component | cytoplasm |
| R | 0006006 | biological_process | glucose metabolic process |
| R | 0006096 | biological_process | glycolytic process |
| R | 0016491 | molecular_function | oxidoreductase activity |
| R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| R | 0050661 | molecular_function | NADP binding |
| R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 R 337 |
| Chain | Residue |
| R | SER150 |
| R | CYS151 |
| R | THR152 |
| R | HIS178 |
| R | THR211 |
| R | GLY212 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 P 337 |
| Chain | Residue |
| P | HIS178 |
| P | THR211 |
| P | GLY212 |
| P | HOH369 |
| P | SER150 |
| P | CYS151 |
| P | THR152 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 O 337 |
| Chain | Residue |
| O | SER150 |
| O | CYS151 |
| O | THR152 |
| O | HIS178 |
| O | THR211 |
| O | GLY212 |
| O | HOH339 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 Q 337 |
| Chain | Residue |
| Q | SER150 |
| Q | CYS151 |
| Q | THR152 |
| Q | HIS178 |
| Q | THR211 |
| Q | GLY212 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of Staphylococcal GAPDH1 in a hexagonal space group.","authors":["Roychowdhury A.","Mukherjee S.","Dutta D.","Das A.K."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






