2HLP
CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate metabolic process |
| 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 activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016491 | molecular_function | oxidoreductase 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 activity |
Functional Information from PDB Data
| site_id | 1 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| A | LYS205 |
| A | GLU188 |
| A | ARG207 |
| A | ASP211 |
| site_id | 2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| B | LYS205 |
| B | GLU188 |
| B | ARG207 |
| B | ASP211 |
| site_id | 3 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| B | GLU247 |
| A | GLU247 |
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1001 |
| Chain | Residue |
| A | THR210 |
| A | ASP211 |
| B | LYS205 |
| B | ASP306 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1002 |
| Chain | Residue |
| A | LYS205 |
| A | ASP306 |
| B | ASP211 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 2001 |
| Chain | Residue |
| A | GLU247 |
| B | GLU247 |
| B | HOH1025 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889 |
| Chain | Residue | Details |
| A | HIS195 | |
| B | HIS195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12581646 |
| Chain | Residue | Details |
| A | GLY28 | |
| A | ASP53 | |
| A | ASN116 | |
| A | THR138 | |
| B | GLY28 | |
| B | ASP53 | |
| B | ASN116 | |
| B | THR138 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P61889 |
| Chain | Residue | Details |
| A | ARG102 | |
| A | ARG109 | |
| A | ASN140 | |
| A | ARG171 | |
| B | ARG102 | |
| B | ARG109 | |
| B | ASN140 | |
| B | ARG171 |
