3LC2
Crystal Structure of Thioacyl-Glyceraldehyde-3-phosphate dehydrogenase 1(GAPDH 1) from methicillin resistant Staphylococcus aureus MRSA252
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 G3H O 337 | 
| Chain | Residue | 
| O | SER150 | 
| O | CYS151 | 
| O | THR152 | 
| O | HIS178 | 
| O | THR211 | 
| O | GLY212 | 
| site_id | AC2 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE GOL O 339 | 
| Chain | Residue | 
| O | GLY11 | 
| O | ARG12 | 
| site_id | AC3 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE G3H Q 337 | 
| Chain | Residue | 
| Q | CYS151 | 
| Q | THR152 | 
| Q | HIS178 | 
| Q | THR211 | 
| Q | GLY212 | 
| Q | HOH350 | 
| Q | SER150 | 
| site_id | AC4 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE GOL Q 339 | 
| Chain | Residue | 
| Q | GLY11 | 
| Q | ARG12 | 
| Q | HOH352 | 
| site_id | AC5 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE G3H R 337 | 
| Chain | Residue | 
| R | SER150 | 
| R | CYS151 | 
| R | THR152 | 
| R | HIS178 | 
| R | THR181 | 
| R | THR211 | 
| R | GLY212 | 
| site_id | AC6 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE GOL R 339 | 
| Chain | Residue | 
| R | GLY11 | 
| R | ARG12 | 
| R | ILE13 | 
| R | HOH374 | 
| site_id | AC7 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE G3H P 337 | 
| Chain | Residue | 
| P | SER150 | 
| P | CYS151 | 
| P | THR152 | 
| P | HIS178 | 
| P | THR181 | 
| P | THR211 | 
| P | GLY212 | 
| P | HOH363 | 
| P | HOH370 | 
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 | 











