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 | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | HIS177 | |
B | HIS177 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY7 | |
B | GLY7 | |
B | ASP34 | |
B | ARG81 | |
B | ARG87 | |
B | ASN94 | |
B | ILE117 | |
B | ASN119 | |
B | ARG153 | |
B | MET227 | |
A | ASP34 | |
A | ARG81 | |
A | ARG87 | |
A | ASN94 | |
A | ILE117 | |
A | ASN119 | |
A | ARG153 | |
A | MET227 |