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6MV8

LDHA structure in complex with inhibitor 14

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate 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
A0019752biological_processcarboxylic acid metabolic process
A0042802molecular_functionidentical protein binding
A0045296molecular_functioncadherin binding
A0070062cellular_componentextracellular exosome
A1990204cellular_componentoxidoreductase complex
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006089biological_processlactate metabolic process
B0006090biological_processpyruvate 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
B0019752biological_processcarboxylic acid metabolic process
B0042802molecular_functionidentical protein binding
B0045296molecular_functioncadherin binding
B0070062cellular_componentextracellular exosome
B1990204cellular_componentoxidoreductase complex
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006089biological_processlactate metabolic process
C0006090biological_processpyruvate 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
C0019752biological_processcarboxylic acid metabolic process
C0042802molecular_functionidentical protein binding
C0045296molecular_functioncadherin binding
C0070062cellular_componentextracellular exosome
C1990204cellular_componentoxidoreductase complex
D0003824molecular_functioncatalytic activity
D0004459molecular_functionL-lactate dehydrogenase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006089biological_processlactate metabolic process
D0006090biological_processpyruvate 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
D0019752biological_processcarboxylic acid metabolic process
D0042802molecular_functionidentical protein binding
D0045296molecular_functioncadherin binding
D0070062cellular_componentextracellular exosome
D1990204cellular_componentoxidoreductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue NAI A 801
ChainResidue
AGLY28
AILE115
AILE119
AVAL135
ASER136
AASN137
AHIS192
ATHR247
AILE251
AD3S804
AHOH907
AALA29
AHOH909
AHOH922
AHOH925
AHOH973
AHOH1003
AHOH1009
AHOH1046
AHOH1051
AVAL30
AASP51
AVAL52
AILE53
ATHR94
AALA95
AGLY96

site_idAC2
Number of Residues5
Detailsbinding site for residue EPE A 802
ChainResidue
ATRP147
AGLY151
APHE152
APRO153
ALYS154

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 803
ChainResidue
AARG170
AHIS185
AHOH920
AHOH970
AHOH1007
CHIS185

site_idAC4
Number of Residues12
Detailsbinding site for residue D3S A 804
ChainResidue
AASN137
AASP165
AARG168
AHIS192
AGLY193
AVAL233
AALA237
ATYR238
AILE241
ATHR247
ANAI801
AHOH925

site_idAC5
Number of Residues29
Detailsbinding site for residue NAI B 801
ChainResidue
BGLY28
BALA29
BVAL30
BASP51
BVAL52
BILE53
BLYS56
BTHR94
BALA95
BGLY96
BALA97
BARG98
BILE115
BILE119
BVAL135
BASN137
BSER160
BLEU164
BHIS192
BTHR247
BILE251
BLAC804
BHOH904
BHOH920
BHOH921
BHOH936
BHOH1008
BHOH1018
BHOH1034

site_idAC6
Number of Residues5
Detailsbinding site for residue EPE B 802
ChainResidue
ALYS283
BTRP147
BPHE152
BPRO153
BLYS154

site_idAC7
Number of Residues9
Detailsbinding site for residue SO4 B 803
ChainResidue
BARG170
BHIS185
BHOH929
BHOH966
BHOH968
BHOH1024
BHOH1033
DHIS185
DHOH917

site_idAC8
Number of Residues6
Detailsbinding site for residue LAC B 804
ChainResidue
BASN137
BARG168
BHIS192
BTHR247
BNAI801
BHOH944

site_idAC9
Number of Residues19
Detailsbinding site for residue NAI C 801
ChainResidue
CGLY28
CALA29
CVAL30
CASP51
CVAL52
CILE53
CTHR94
CALA95
CILE115
CVAL135
CASN137
CHIS192
CTHR247
CILE251
CD3S804
CHOH904
CHOH915
CHOH972
CHOH987

site_idAD1
Number of Residues5
Detailsbinding site for residue EPE C 802
ChainResidue
CTRP147
CGLY151
CPHE152
CPRO153
CLYS154

site_idAD2
Number of Residues6
Detailsbinding site for residue SO4 C 803
ChainResidue
AHIS185
CARG170
CHIS185
CHOH902
CHOH951
CHOH986

site_idAD3
Number of Residues13
Detailsbinding site for residue D3S C 804
ChainResidue
CASN137
CASP165
CARG168
CHIS192
CGLY193
CASP194
CALA237
CTYR238
CILE241
CTHR247
CNAI801
CHOH915
CHOH1001

site_idAD4
Number of Residues28
Detailsbinding site for residue NAI D 801
ChainResidue
DGLY28
DALA29
DVAL30
DASP51
DVAL52
DILE53
DTHR94
DALA95
DGLY96
DALA97
DARG98
DILE115
DILE119
DVAL135
DSER136
DASN137
DHIS192
DILE251
DD3S802
DHOH944
DHOH951
DHOH965
DHOH966
DHOH967
DHOH993
DHOH1016
DHOH1041
DHOH1057

site_idAD5
Number of Residues13
Detailsbinding site for residue D3S D 802
ChainResidue
DARG98
DASN137
DASP165
DARG168
DHIS192
DGLY193
DALA237
DTYR238
DILE241
DTHR247
DNAI801
DHOH966
DHOH997

site_idAD6
Number of Residues8
Detailsbinding site for residue SO4 D 803
ChainResidue
BHIS185
BHOH926
DARG170
DHIS185
DHOH905
DHOH931
DHOH948
DHOH1001

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS192
BHIS192
CHIS192
DHIS192

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11276087
ChainResidueDetails
AGLY28
AARG98
BGLY28
BARG98
CGLY28
CARG98
DGLY28
DARG98

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AARG105
CASN137
CARG168
CTHR247
DARG105
DASN137
DARG168
DTHR247
AASN137
AARG168
ATHR247
BARG105
BASN137
BARG168
BTHR247
CARG105

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AALA1
BALA1
CALA1
DALA1

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
ChainResidueDetails
ALYS4
DLYS4
DLYS117
DLYS317
ALYS117
ALYS317
BLYS4
BLYS117
BLYS317
CLYS4
CLYS117
CLYS317

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR9
BTYR9
CTYR9
DTYR9

site_idSWS_FT_FI7
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS13
DLYS13
DLYS80
DLYS125
ALYS80
ALYS125
BLYS13
BLYS80
BLYS125
CLYS13
CLYS80
CLYS125

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR17
BTHR17
CTHR17
DTHR17

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS56
BLYS56
CLYS56
DLYS56

site_idSWS_FT_FI10
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06151
ChainResidueDetails
ALYS223
DLYS223
DLYS231
DLYS242
ALYS231
ALYS242
BLYS223
BLYS231
BLYS242
CLYS223
CLYS231
CLYS242

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06151
ChainResidueDetails
ATYR238
BTYR238
CTYR238
DTYR238

site_idSWS_FT_FI12
Number of Residues8
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04642
ChainResidueDetails
ATHR308
ATHR321
BTHR308
BTHR321
CTHR308
CTHR321
DTHR308
DTHR321

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER309
BSER309
CSER309
DSER309

site_idSWS_FT_FI14
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS56
BLYS56
CLYS56
DLYS56

223166

PDB entries from 2024-07-31

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