6AOO
2.15 Angstrom Resolution Crystal Structure of Malate Dehydrogenase from Haemophilus influenzae
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 | 0006108 | biological_process | malate metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016615 | molecular_function | malate dehydrogenase 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016615 | molecular_function | malate dehydrogenase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | ARG81 |
| A | ARG153 |
| A | GLY210 |
| A | ALA223 |
| A | MET227 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | HOH600 |
| A | TYR138 |
| A | ASP139 |
| A | LYS140 |
| A | ARG141 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | SER167 |
| A | ARG168 |
| A | HOH552 |
| B | ARG236 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | ARG153 |
| B | GLY210 |
| B | SER222 |
| B | ALA223 |
| B | MET227 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | SER167 |
| B | ARG168 |
| B | HOH565 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | LYS133 |
| B | GLY136 |
| B | VAL137 |
| B | TYR138 |
| B | HOH545 |
| B | HOH552 |
Functional Information from PROSITE/UniProt
| site_id | PS00068 |
| Number of Residues | 13 |
| Details | MDH Malate dehydrogenase active site signature. VTTLDvlRSetfV |
| Chain | Residue | Details |
| A | VAL146-VAL158 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 29 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
