1I0Z
HUMAN HEART L-LACTATE DEHYDROGENASE H CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004457 | molecular_function | lactate dehydrogenase activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0016020 | cellular_component | membrane |
| 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 | 0019674 | biological_process | NAD+ metabolic process |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0019900 | molecular_function | kinase binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042867 | biological_process | pyruvate catabolic process |
| A | 0045121 | cellular_component | membrane raft |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1990204 | cellular_component | oxidoreductase complex |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004457 | molecular_function | lactate dehydrogenase activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005829 | cellular_component | cytosol |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0016020 | cellular_component | membrane |
| 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 | 0019674 | biological_process | NAD+ metabolic process |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0019900 | molecular_function | kinase binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042867 | biological_process | pyruvate catabolic process |
| B | 0045121 | cellular_component | membrane raft |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAI A 401 |
| Chain | Residue |
| A | GLY29 |
| A | VAL98 |
| A | ARG99 |
| A | VAL136 |
| A | SER137 |
| A | ASN138 |
| A | SER161 |
| A | LEU165 |
| A | HIS193 |
| A | THR248 |
| A | ILE252 |
| A | GLN30 |
| A | OXM402 |
| A | HOH410 |
| A | HOH413 |
| A | HOH454 |
| A | HOH462 |
| A | HOH477 |
| A | HOH480 |
| A | HOH498 |
| A | HOH500 |
| A | HOH502 |
| A | VAL31 |
| A | HOH503 |
| A | HOH523 |
| A | HOH546 |
| A | ASP52 |
| A | VAL53 |
| A | LEU54 |
| A | THR95 |
| A | ALA96 |
| A | GLY97 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXM A 402 |
| Chain | Residue |
| A | GLN100 |
| A | ARG106 |
| A | ASN138 |
| A | ARG169 |
| A | HIS193 |
| A | ALA238 |
| A | THR248 |
| A | NAI401 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAI B 411 |
| Chain | Residue |
| A | ASN108 |
| B | GLY29 |
| B | GLN30 |
| B | VAL31 |
| B | ASP52 |
| B | VAL53 |
| B | LEU54 |
| B | THR95 |
| B | ALA96 |
| B | GLY97 |
| B | VAL98 |
| B | ARG99 |
| B | ILE120 |
| B | VAL136 |
| B | ASN138 |
| B | SER161 |
| B | LEU165 |
| B | HIS193 |
| B | THR248 |
| B | ILE252 |
| B | OXM412 |
| B | HOH419 |
| B | HOH433 |
| B | HOH438 |
| B | HOH470 |
| B | HOH480 |
| B | HOH498 |
| B | HOH534 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OXM B 412 |
| Chain | Residue |
| B | GLN100 |
| B | ARG106 |
| B | ASN138 |
| B | ARG169 |
| B | HIS193 |
| B | ALA238 |
| B | THR248 |
| B | NAI411 |
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 | LEU190-SER196 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11276087","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | ASP166 | |
| A | HIS193 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | ASP166 | |
| B | HIS193 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS193 | |
| A | ASP166 | |
| A | ARG169 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS193 | |
| B | ASP166 | |
| B | ARG169 |
