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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9BK2

Crystal structure of Lactate dehydrogenase in complex with 4-((4-(1-methyl-1H-imidazole-2-carbonyl)phenyl)amino)-4-oxo-2-(4-(trifluoromethyl)phenyl)butanoic acid (S-enantiomer, monoclinic P form)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004457molecular_functionlactate dehydrogenase activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006089biological_processlactate metabolic process
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019661biological_processglucose catabolic process to lactate via pyruvate
A0019752biological_processcarboxylic acid metabolic process
A0035686cellular_componentsperm fibrous sheath
A0042802molecular_functionidentical protein binding
A0042867biological_processpyruvate catabolic process
A0045296molecular_functioncadherin binding
A0070062cellular_componentextracellular exosome
A1990204cellular_componentoxidoreductase complex
B0003824molecular_functioncatalytic activity
B0004457molecular_functionlactate dehydrogenase activity
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006089biological_processlactate metabolic process
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019661biological_processglucose catabolic process to lactate via pyruvate
B0019752biological_processcarboxylic acid metabolic process
B0035686cellular_componentsperm fibrous sheath
B0042802molecular_functionidentical protein binding
B0042867biological_processpyruvate catabolic process
B0045296molecular_functioncadherin binding
B0070062cellular_componentextracellular exosome
B1990204cellular_componentoxidoreductase complex
C0003824molecular_functioncatalytic activity
C0004457molecular_functionlactate dehydrogenase activity
C0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006089biological_processlactate metabolic process
C0006096biological_processglycolytic process
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019661biological_processglucose catabolic process to lactate via pyruvate
C0019752biological_processcarboxylic acid metabolic process
C0035686cellular_componentsperm fibrous sheath
C0042802molecular_functionidentical protein binding
C0042867biological_processpyruvate catabolic process
C0045296molecular_functioncadherin binding
C0070062cellular_componentextracellular exosome
C1990204cellular_componentoxidoreductase complex
D0003824molecular_functioncatalytic activity
D0004457molecular_functionlactate dehydrogenase activity
D0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006089biological_processlactate metabolic process
D0006096biological_processglycolytic process
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019661biological_processglucose catabolic process to lactate via pyruvate
D0019752biological_processcarboxylic acid metabolic process
D0035686cellular_componentsperm fibrous sheath
D0042802molecular_functionidentical protein binding
D0042867biological_processpyruvate catabolic process
D0045296molecular_functioncadherin binding
D0070062cellular_componentextracellular exosome
D1990204cellular_componentoxidoreductase complex
Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. LGEHGDS
ChainResidueDetails
ALEU189-SER195
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues116
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11276087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsModified 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"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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