5YTA
Pig Heart Lactate Dehydrogenase in complex with NADH and Oxamate
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 | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0006089 | biological_process | lactate metabolic process |
A | 0006090 | biological_process | pyruvate metabolic 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 | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0006089 | biological_process | lactate metabolic process |
B | 0006090 | biological_process | pyruvate metabolic 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 | 31 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | GLY30 |
A | VAL99 |
A | ARG100 |
A | VAL117 |
A | ILE121 |
A | VAL137 |
A | SER138 |
A | ASN139 |
A | SER162 |
A | LEU166 |
A | HIS194 |
A | GLN31 |
A | THR249 |
A | ILE253 |
A | OXM402 |
A | HOH506 |
A | HOH520 |
A | HOH521 |
A | HOH533 |
A | HOH534 |
A | HOH536 |
A | HOH545 |
A | VAL32 |
A | HOH547 |
A | HOH566 |
A | ASP53 |
A | VAL54 |
A | LEU55 |
A | THR96 |
A | ALA97 |
A | GLY98 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue OXM A 402 |
Chain | Residue |
A | GLN101 |
A | ARG107 |
A | ASN139 |
A | ARG170 |
A | HIS194 |
A | ALA239 |
A | THR249 |
A | NAD401 |
site_id | AC3 |
Number of Residues | 29 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
B | GLY30 |
B | GLN31 |
B | VAL32 |
B | ASP53 |
B | VAL54 |
B | LEU55 |
B | THR96 |
B | ALA97 |
B | GLY98 |
B | VAL99 |
B | ARG100 |
B | VAL117 |
B | VAL137 |
B | SER138 |
B | ASN139 |
B | SER162 |
B | LEU166 |
B | HIS194 |
B | THR249 |
B | ILE253 |
B | OXM402 |
B | HOH501 |
B | HOH504 |
B | HOH509 |
B | HOH510 |
B | HOH515 |
B | HOH524 |
B | HOH540 |
B | HOH551 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue OXM B 402 |
Chain | Residue |
B | GLN101 |
B | ARG107 |
B | ASN139 |
B | LEU166 |
B | ARG170 |
B | HIS194 |
B | ALA239 |
B | THR249 |
B | NAD401 |
Functional Information from PROSITE/UniProt
site_id | PS00064 |
Number of Residues | 7 |
Details | L_LDH L-lactate dehydrogenase active site. LGEHGDS |
Chain | Residue | Details |
A | LEU191-SER197 |
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 | HIS194 | |
B | HIS194 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY30 | |
B | ASN139 | |
B | ARG170 | |
B | THR249 | |
A | ARG100 | |
A | ARG107 | |
A | ASN139 | |
A | ARG170 | |
A | THR249 | |
B | GLY30 | |
B | ARG100 | |
B | ARG107 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:838465 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07195 |
Chain | Residue | Details |
A | LYS7 | |
A | LYS58 | |
A | LYS119 | |
A | LYS329 | |
B | LYS7 | |
B | LYS58 | |
B | LYS119 | |
B | LYS329 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07195 |
Chain | Residue | Details |
A | SER44 | |
B | SER44 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07195 |
Chain | Residue | Details |
A | TYR240 | |
B | TYR240 |