6H9S
Crystal dimeric structure of Petrotoga mobilis lactate dehydrogenase with NADH
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 | 0006096 | biological_process | glycolytic process |
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 |
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 | 0006096 | biological_process | glycolytic process |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | GLY9 |
A | ILE115 |
A | ASN117 |
A | THR140 |
A | HIS172 |
A | THR228 |
A | HOH507 |
A | HOH513 |
A | HOH521 |
A | HOH523 |
A | HOH533 |
A | ARG10 |
A | HOH550 |
A | HOH551 |
A | HOH563 |
A | HOH575 |
A | VAL11 |
A | ASP32 |
A | LEU33 |
A | THR74 |
A | ALA75 |
A | GLY76 |
A | ILE95 |
site_id | AC2 |
Number of Residues | 24 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
B | GLY9 |
B | ARG10 |
B | VAL11 |
B | ASP32 |
B | LEU33 |
B | THR74 |
B | ALA75 |
B | GLY76 |
B | ALA77 |
B | ALA78 |
B | ILE95 |
B | ILE115 |
B | ASN117 |
B | THR140 |
B | HIS172 |
B | THR228 |
B | HOH512 |
B | HOH515 |
B | HOH528 |
B | HOH532 |
B | HOH533 |
B | HOH545 |
B | HOH555 |
B | HOH580 |
Functional Information from PROSITE/UniProt
site_id | PS00064 |
Number of Residues | 7 |
Details | L_LDH L-lactate dehydrogenase active site. IGEHGDS |
Chain | Residue | Details |
A | ILE169-SER175 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | HIS172 | |
B | HIS172 |
site_id | SWS_FT_FI2 |
Number of Residues | 26 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | VAL11 | |
A | ASP145 | |
A | ARG150 | |
A | HIS165 | |
A | THR228 | |
B | VAL11 | |
B | ASP32 | |
B | TYR62 | |
B | GLY76 | |
B | GLN79 | |
B | ARG85 | |
A | ASP32 | |
B | ILE115 | |
B | ASN117 | |
B | THR140 | |
B | ASP145 | |
B | ARG150 | |
B | HIS165 | |
B | THR228 | |
A | TYR62 | |
A | GLY76 | |
A | GLN79 | |
A | ARG85 | |
A | ILE115 | |
A | ASN117 | |
A | THR140 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | TYR219 | |
B | TYR219 |