6BAX
Lactate Dehydrogenase in complex with inhibitor 6-(3-aminophenyl)-3-((2-chlorophenyl)thio)-4-hydroxy-6-(thiophen-3-yl)-5,6-dihydro-2H-pyran-2-one
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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006096 | biological_process | glycolytic 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 | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0035686 | cellular_component | sperm fibrous sheath |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042867 | biological_process | pyruvate catabolic process |
| A | 0045296 | molecular_function | cadherin 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 | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006096 | biological_process | glycolytic 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 | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0035686 | cellular_component | sperm fibrous sheath |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042867 | biological_process | pyruvate catabolic process |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1990204 | cellular_component | oxidoreductase complex |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004457 | molecular_function | lactate dehydrogenase activity |
| C | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005829 | cellular_component | cytosol |
| C | 0006089 | biological_process | lactate metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0035686 | cellular_component | sperm fibrous sheath |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042867 | biological_process | pyruvate catabolic process |
| C | 0045296 | molecular_function | cadherin binding |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 1990204 | cellular_component | oxidoreductase complex |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004457 | molecular_function | lactate dehydrogenase activity |
| D | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005829 | cellular_component | cytosol |
| D | 0006089 | biological_process | lactate metabolic process |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0019661 | biological_process | glucose catabolic process to lactate via pyruvate |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0035686 | cellular_component | sperm fibrous sheath |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042867 | biological_process | pyruvate catabolic process |
| D | 0045296 | molecular_function | cadherin binding |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue NAD A 801 |
| Chain | Residue |
| A | GLY28 |
| A | ILE115 |
| A | ILE119 |
| A | VAL135 |
| A | ASN137 |
| A | HIS192 |
| A | THR247 |
| A | ILE251 |
| A | D4S804 |
| A | HOH904 |
| A | HOH919 |
| A | ALA29 |
| A | HOH971 |
| A | VAL30 |
| A | ASP51 |
| A | VAL52 |
| A | ILE53 |
| A | THR94 |
| A | ALA95 |
| A | GLY96 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EPE A 802 |
| Chain | Residue |
| A | TRP147 |
| A | GLY151 |
| A | PHE152 |
| A | LYS154 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 803 |
| Chain | Residue |
| A | ARG170 |
| A | HIS185 |
| A | HOH925 |
| A | HOH1012 |
| A | HOH1020 |
| C | LEU182 |
| C | HIS185 |
| C | HOH962 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue D4S A 804 |
| Chain | Residue |
| A | VAL30 |
| A | ASN137 |
| A | ASP165 |
| A | ARG168 |
| A | HIS192 |
| A | GLY193 |
| A | ALA237 |
| A | TYR238 |
| A | ILE241 |
| A | TYR246 |
| A | THR247 |
| A | NAD801 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | binding site for residue NAD B 801 |
| Chain | Residue |
| B | GLY28 |
| B | ALA29 |
| B | VAL30 |
| B | ASP51 |
| B | VAL52 |
| B | ILE53 |
| B | THR94 |
| B | ALA95 |
| B | GLY96 |
| B | ILE115 |
| B | ILE119 |
| B | VAL135 |
| B | ASN137 |
| B | SER160 |
| B | HIS192 |
| B | THR247 |
| B | ILE251 |
| B | D4S803 |
| B | HOH901 |
| B | HOH905 |
| B | HOH944 |
| B | HOH962 |
| B | HOH971 |
| B | HOH992 |
| B | HOH1018 |
| B | HOH1022 |
| B | HOH1031 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EPE B 802 |
| Chain | Residue |
| A | LYS283 |
| B | TRP147 |
| B | GLY151 |
| B | PRO153 |
| B | LYS154 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue D4S B 803 |
| Chain | Residue |
| B | VAL30 |
| B | ASN137 |
| B | ASP165 |
| B | ARG168 |
| B | HIS192 |
| B | GLY193 |
| B | VAL234 |
| B | ALA237 |
| B | TYR238 |
| B | ILE241 |
| B | TYR246 |
| B | THR247 |
| B | NAD801 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue NAD C 801 |
| Chain | Residue |
| C | ASN137 |
| C | HIS192 |
| C | THR247 |
| C | ILE251 |
| C | D4S803 |
| C | HOH905 |
| C | HOH917 |
| C | HOH931 |
| C | HOH979 |
| C | HOH1010 |
| C | GLY28 |
| C | ALA29 |
| C | VAL30 |
| C | ASP51 |
| C | VAL52 |
| C | ILE53 |
| C | THR94 |
| C | ALA95 |
| C | ILE119 |
| C | VAL135 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EPE C 802 |
| Chain | Residue |
| C | TRP147 |
| C | GLY151 |
| C | PRO153 |
| C | LYS154 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue D4S C 803 |
| Chain | Residue |
| C | VAL30 |
| C | ASN137 |
| C | ASP165 |
| C | ARG168 |
| C | HIS192 |
| C | GLY193 |
| C | ALA237 |
| C | TYR238 |
| C | ILE241 |
| C | TYR246 |
| C | THR247 |
| C | NAD801 |
| C | HOH933 |
| site_id | AD2 |
| Number of Residues | 25 |
| Details | binding site for residue NAD D 801 |
| Chain | Residue |
| D | GLY28 |
| D | ALA29 |
| D | VAL30 |
| D | ASP51 |
| D | VAL52 |
| D | ILE53 |
| D | THR94 |
| D | ALA95 |
| D | GLY96 |
| D | ILE115 |
| D | ILE119 |
| D | VAL135 |
| D | SER136 |
| D | ASN137 |
| D | HIS192 |
| D | THR247 |
| D | ILE251 |
| D | D4S803 |
| D | HOH902 |
| D | HOH925 |
| D | HOH949 |
| D | HOH956 |
| D | HOH982 |
| D | HOH1017 |
| D | HOH1035 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 D 802 |
| Chain | Residue |
| B | LEU182 |
| B | HIS185 |
| D | ARG170 |
| D | HIS185 |
| D | HOH919 |
| D | HOH1014 |
| D | HOH1027 |
| D | HOH1049 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for residue D4S D 803 |
| Chain | Residue |
| D | VAL30 |
| D | ASN137 |
| D | ASP165 |
| D | ARG168 |
| D | HIS192 |
| D | GLY193 |
| D | ALA237 |
| D | TYR238 |
| D | ILE241 |
| D | TYR246 |
| D | THR247 |
| D | NAD801 |
| D | HOH1021 |
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 | LEU189-SER195 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 112 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11276087","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
