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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4AJJ

rat LDHA in complex with 2-((3,4-dimethoxyphenyl)methyl))propanedioic acid and N-(2-methyl-1,3-benzothiazol-6-yl)-3-ureido-propanamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0001889biological_processliver development
A0003824molecular_functioncatalytic activity
A0004457molecular_functionlactate dehydrogenase activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006089biological_processlactate metabolic process
A0007519biological_processskeletal muscle tissue development
A0007584biological_processresponse to nutrient
A0009410biological_processresponse to xenobiotic stimulus
A0009749biological_processresponse to glucose
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
A0019674biological_processNAD+ metabolic process
A0019752biological_processcarboxylic acid metabolic process
A0019900molecular_functionkinase binding
A0035686cellular_componentsperm fibrous sheath
A0042542biological_processresponse to hydrogen peroxide
A0042802molecular_functionidentical protein binding
A0042867biological_processpyruvate catabolic process
A0043065biological_processpositive regulation of apoptotic process
A0043627biological_processresponse to estrogen
A0051287molecular_functionNAD binding
A0051591biological_processresponse to cAMP
A1904628biological_processcellular response to phorbol 13-acetate 12-myristate
A1990204cellular_componentoxidoreductase complex
B0001666biological_processresponse to hypoxia
B0001889biological_processliver development
B0003824molecular_functioncatalytic activity
B0004457molecular_functionlactate dehydrogenase activity
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006089biological_processlactate metabolic process
B0007519biological_processskeletal muscle tissue development
B0007584biological_processresponse to nutrient
B0009410biological_processresponse to xenobiotic stimulus
B0009749biological_processresponse to glucose
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
B0019674biological_processNAD+ metabolic process
B0019752biological_processcarboxylic acid metabolic process
B0019900molecular_functionkinase binding
B0035686cellular_componentsperm fibrous sheath
B0042542biological_processresponse to hydrogen peroxide
B0042802molecular_functionidentical protein binding
B0042867biological_processpyruvate catabolic process
B0043065biological_processpositive regulation of apoptotic process
B0043627biological_processresponse to estrogen
B0051287molecular_functionNAD binding
B0051591biological_processresponse to cAMP
B1904628biological_processcellular response to phorbol 13-acetate 12-myristate
B1990204cellular_componentoxidoreductase complex
C0001666biological_processresponse to hypoxia
C0001889biological_processliver development
C0003824molecular_functioncatalytic activity
C0004457molecular_functionlactate dehydrogenase activity
C0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006089biological_processlactate metabolic process
C0007519biological_processskeletal muscle tissue development
C0007584biological_processresponse to nutrient
C0009410biological_processresponse to xenobiotic stimulus
C0009749biological_processresponse to glucose
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
C0019674biological_processNAD+ metabolic process
C0019752biological_processcarboxylic acid metabolic process
C0019900molecular_functionkinase binding
C0035686cellular_componentsperm fibrous sheath
C0042542biological_processresponse to hydrogen peroxide
C0042802molecular_functionidentical protein binding
C0042867biological_processpyruvate catabolic process
C0043065biological_processpositive regulation of apoptotic process
C0043627biological_processresponse to estrogen
C0051287molecular_functionNAD binding
C0051591biological_processresponse to cAMP
C1904628biological_processcellular response to phorbol 13-acetate 12-myristate
C1990204cellular_componentoxidoreductase complex
D0001666biological_processresponse to hypoxia
D0001889biological_processliver development
D0003824molecular_functioncatalytic activity
D0004457molecular_functionlactate dehydrogenase activity
D0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006089biological_processlactate metabolic process
D0007519biological_processskeletal muscle tissue development
D0007584biological_processresponse to nutrient
D0009410biological_processresponse to xenobiotic stimulus
D0009749biological_processresponse to glucose
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
D0019674biological_processNAD+ metabolic process
D0019752biological_processcarboxylic acid metabolic process
D0019900molecular_functionkinase binding
D0035686cellular_componentsperm fibrous sheath
D0042542biological_processresponse to hydrogen peroxide
D0042802molecular_functionidentical protein binding
D0042867biological_processpyruvate catabolic process
D0043065biological_processpositive regulation of apoptotic process
D0043627biological_processresponse to estrogen
D0051287molecular_functionNAD binding
D0051591biological_processresponse to cAMP
D1904628biological_processcellular response to phorbol 13-acetate 12-myristate
D1990204cellular_componentoxidoreductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 88S A 1332
ChainResidue
AGLY28
AHOH2037
AHOH2077
AHOH2127
AHOH2135
AASP51
AVAL52
ATHR94
AALA95
AGLY96
APHE118
AILE119
AHOH2034
site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLI A 1333
ChainResidue
AARG105
AASN137
ALEU164
AARG168
AHIS192
AALA237
ATHR247
AHOH2200
AHOH2307
site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 88S B 1332
ChainResidue
BGLY28
BASP51
BVAL52
BTHR94
BALA95
BGLY96
BARG98
BILE119
B88R1333
BHOH2024
BHOH2028
BHOH2093
BHOH2100
site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 88R B 1333
ChainResidue
BVAL30
BTHR94
BGLN99
BARG105
BVAL135
BSER136
BASN137
BLEU164
BARG168
BHIS192
BALA237
BTHR247
B88S1332
BHOH2110
site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS C 1332
ChainResidue
CGLY96
CALA97
C88S1334
site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL C 1333
ChainResidue
BSER201
BGLY202
BASN204
BGLY207
CSER201
CGLY202
CVAL203
CASN204
CGLY207
CSER209
site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 88S C 1334
ChainResidue
CASP51
CVAL52
CTHR94
CALA95
CGLY96
CPHE118
CILE119
CDMS1332
C88R1335
CHOH2020
CHOH2022
CHOH2047
CHOH2091
site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 88R C 1335
ChainResidue
CVAL30
CTHR94
CARG98
CGLN99
CARG105
CVAL135
CSER136
CASN137
CLEU164
CARG168
CHIS192
CALA237
CTHR247
C88S1334
site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 88S D 1332
ChainResidue
DHOH2076
DHOH2082
DGLY28
DASP51
DVAL52
DTHR94
DALA95
DGLY96
DILE119
DHOH2022
DHOH2025
DHOH2047
site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLI D 1333
ChainResidue
DGLN99
DARG105
DASN137
DLEU164
DARG168
DHIS192
DALA237
DTHR247
DHOH2117
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","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues132
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P00338","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","von Kriegsheim A.F.","Kolch W."]}}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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