1UR5
Stabilization of a Tetrameric Malate Dehydrogenase by Introduction of a Disulfide Bridge at the Dimer/Dimer Interface
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A1309 |
| Chain | Residue |
| A | GLU178 |
| A | CL1312 |
| A | HOH2156 |
| A | HOH2157 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A1310 |
| Chain | Residue |
| A | GLU165 |
| C | HOH2203 |
| C | HOH2211 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A1311 |
| Chain | Residue |
| A | GLU277 |
| A | HOH2238 |
| A | ASP200 |
| A | ASP243 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A1312 |
| Chain | Residue |
| A | ASP123 |
| A | ALA124 |
| A | CD1309 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA A1313 |
| Chain | Residue |
| A | HIS19 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD C1310 |
| Chain | Residue |
| C | GLU178 |
| C | HOH2083 |
| C | HOH2113 |
| C | HOH2115 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD C1311 |
| Chain | Residue |
| A | HOH2212 |
| C | GLU165 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD C1312 |
| Chain | Residue |
| A | GLU159 |
| A | HOH2139 |
| C | GLU159 |
| C | HOH2140 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA C1313 |
| Chain | Residue |
| C | HIS19 |
| site_id | BC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD A1308 |
| Chain | Residue |
| A | GLY9 |
| A | GLY11 |
| A | PHE12 |
| A | VAL13 |
| A | ASP33 |
| A | ILE34 |
| A | VAL35 |
| A | TYR65 |
| A | THR77 |
| A | SER78 |
| A | GLY79 |
| A | VAL118 |
| A | ASN119 |
| A | ASN120 |
| A | LEU147 |
| A | HIS175 |
| A | ALA225 |
| A | PRO229 |
| A | HOH2277 |
| A | HOH2278 |
| A | HOH2279 |
| A | HOH2280 |
| A | HOH2281 |
| A | HOH2282 |
| site_id | BC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD C1309 |
| Chain | Residue |
| C | GLY9 |
| C | GLY11 |
| C | PHE12 |
| C | VAL13 |
| C | ASP33 |
| C | ILE34 |
| C | VAL35 |
| C | TYR65 |
| C | THR77 |
| C | SER78 |
| C | GLY79 |
| C | ALA80 |
| C | CYS102 |
| C | VAL118 |
| C | ASN120 |
| C | LEU147 |
| C | HIS175 |
| C | PRO229 |
| C | HOH2197 |
| C | HOH2262 |
| C | HOH2263 |
| C | HOH2264 |
| C | HOH2265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12054817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14636605","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS175 | |
| A | ASP148 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS175 | |
| C | ASP148 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS175 | |
| A | ASP148 | |
| A | ARG151 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| C | HIS175 | |
| C | ASP148 | |
| C | ARG151 |
