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 | ASN116 | |
A | THR138 | |
B | GLY28 | |
B | ASP53 | |
B | ASN116 | |
B | THR138 | |
A | GLY28 | |
A | ASP53 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P61889 |
Chain | Residue | Details |
B | ARG102 | |
B | ARG109 | |
B | ASN140 | |
B | ARG171 | |
A | ARG102 | |
A | ARG109 | |
A | ASN140 | |
A | ARG171 |