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1I10

HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE

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
E0003824molecular_functioncatalytic activity
E0004457molecular_functionlactate dehydrogenase activity
E0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005829cellular_componentcytosol
E0006089biological_processlactate metabolic process
E0006096biological_processglycolytic process
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0019661biological_processglucose catabolic process to lactate via pyruvate
E0019752biological_processcarboxylic acid metabolic process
E0035686cellular_componentsperm fibrous sheath
E0042802molecular_functionidentical protein binding
E0042867biological_processpyruvate catabolic process
E0045296molecular_functioncadherin binding
E0070062cellular_componentextracellular exosome
E1990204cellular_componentoxidoreductase complex
F0003824molecular_functioncatalytic activity
F0004457molecular_functionlactate dehydrogenase activity
F0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005739cellular_componentmitochondrion
F0005829cellular_componentcytosol
F0006089biological_processlactate metabolic process
F0006096biological_processglycolytic process
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0019661biological_processglucose catabolic process to lactate via pyruvate
F0019752biological_processcarboxylic acid metabolic process
F0035686cellular_componentsperm fibrous sheath
F0042802molecular_functionidentical protein binding
F0042867biological_processpyruvate catabolic process
F0045296molecular_functioncadherin binding
F0070062cellular_componentextracellular exosome
F1990204cellular_componentoxidoreductase complex
G0003824molecular_functioncatalytic activity
G0004457molecular_functionlactate dehydrogenase activity
G0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005739cellular_componentmitochondrion
G0005829cellular_componentcytosol
G0006089biological_processlactate metabolic process
G0006096biological_processglycolytic process
G0016020cellular_componentmembrane
G0016491molecular_functionoxidoreductase activity
G0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G0019661biological_processglucose catabolic process to lactate via pyruvate
G0019752biological_processcarboxylic acid metabolic process
G0035686cellular_componentsperm fibrous sheath
G0042802molecular_functionidentical protein binding
G0042867biological_processpyruvate catabolic process
G0045296molecular_functioncadherin binding
G0070062cellular_componentextracellular exosome
G1990204cellular_componentoxidoreductase complex
H0003824molecular_functioncatalytic activity
H0004457molecular_functionlactate dehydrogenase activity
H0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0005739cellular_componentmitochondrion
H0005829cellular_componentcytosol
H0006089biological_processlactate metabolic process
H0006096biological_processglycolytic process
H0016020cellular_componentmembrane
H0016491molecular_functionoxidoreductase activity
H0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H0019661biological_processglucose catabolic process to lactate via pyruvate
H0019752biological_processcarboxylic acid metabolic process
H0035686cellular_componentsperm fibrous sheath
H0042802molecular_functionidentical protein binding
H0042867biological_processpyruvate catabolic process
H0045296molecular_functioncadherin binding
H0070062cellular_componentextracellular exosome
H1990204cellular_componentoxidoreductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 803
ChainResidue
AARG170
AHIS185
AHOH898
AHOH900
AHOH907
CLEU182
CHIS185

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 806
ChainResidue
BHOH839
BHOH848
BHOH891
DHIS185
BARG170
BHIS185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT C 809
ChainResidue
AHIS185
AHOH895
AHOH928
CARG170
CHIS185
CHOH854

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT D 812
ChainResidue
BHIS185
BHOH816
DARG170
DHIS185
DHOH825
DHOH855

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT E 815
ChainResidue
EARG170
EHIS185
ETRP187
GHIS185

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT F 818
ChainResidue
FARG170
FHIS185
FHOH822
FHOH838
HHIS185

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT G 821
ChainResidue
ELEU182
EHIS185
GARG170
GHIS185
GTRP187
GHOH822
GHOH834

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT H 824
ChainResidue
FHIS185
HARG170
HHIS185

site_idAC9
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAI A 801
ChainResidue
AGLY28
AALA29
AVAL30
AASP51
AVAL52
AILE53
ALYS56
ATHR94
AALA95
AGLY96
AALA97
AARG98
AILE119
AVAL135
AASN137
ASER160
ALEU164
AHIS192
ATHR247
AILE251
AOXM802
AHOH804
AHOH807
AHOH814
AHOH826
AHOH851
AHOH864
AHOH877
AHOH885

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OXM A 802
ChainResidue
AGLN99
AARG105
AASN137
ALEU164
AARG168
AHIS192
AALA237
ATHR247
ANAI801

site_idBC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAI B 804
ChainResidue
BSER160
BLEU164
BHIS192
BTHR247
BILE251
BOXM805
BHOH812
BHOH814
BHOH831
BHOH855
BHOH907
BHOH916
BHOH929
FASN107
BGLY28
BALA29
BVAL30
BASP51
BVAL52
BILE53
BLYS56
BTHR94
BALA95
BGLY96
BALA97
BARG98
BILE115
BILE119
BVAL135
BSER136
BASN137

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OXM B 805
ChainResidue
BGLN99
BARG105
BASN137
BARG168
BHIS192
BALA237
BTHR247
BNAI804

site_idBC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAI C 807
ChainResidue
CGLY28
CALA29
CVAL30
CASP51
CVAL52
CILE53
CLYS56
CTHR94
CALA95
CGLY96
CALA97
CARG98
CILE119
CVAL135
CASN137
CSER160
CLEU164
CHIS192
CTHR247
CILE251
COXM808
CHOH836
CHOH855
CHOH856
CHOH857
CHOH861
HASN107

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OXM C 808
ChainResidue
CGLN99
CARG105
CASN137
CARG168
CHIS192
CALA237
CTHR247
CNAI807

site_idBC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAI D 810
ChainResidue
DGLY26
DGLY28
DALA29
DVAL30
DASP51
DVAL52
DILE53
DTHR94
DALA95
DGLY96
DARG98
DILE115
DILE119
DVAL135
DASN137
DSER160
DHIS192
DOXM811
DHOH858
DHOH889

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXM D 811
ChainResidue
DASN137
DARG168
DHIS192
DALA237
DTHR247
DNAI810

site_idBC8
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAI E 813
ChainResidue
AGLN110
AHOH937
EGLY28
EALA29
EVAL30
EASP51
EVAL52
ETHR94
EALA95
EGLY96
EVAL135
EASN137
ESER160
ELEU164
EHIS192
ETHR247
EILE251
EOXM814
EHOH839
EHOH847
EHOH851

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OXM E 814
ChainResidue
EASN137
ELEU164
EARG168
EHIS192
EALA237
ETHR247
ENAI813

site_idCC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAI F 816
ChainResidue
FGLY28
FALA29
FVAL30
FASP51
FVAL52
FILE53
FTHR94
FALA95
FGLY96
FALA97
FARG98
FILE115
FVAL135
FASN137
FSER160
FLEU164
FHIS192
FTHR247
FILE251
FOXM817
FHOH832
FHOH837
FHOH845
FHOH851
FHOH861
FHOH862

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OXM F 817
ChainResidue
FGLN99
FARG105
FASN137
FARG168
FHIS192
FALA237
FTHR247
FNAI816

site_idCC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAI G 819
ChainResidue
DGLN330
GGLY28
GALA29
GVAL30
GASP51
GVAL52
GILE53
GTHR94
GALA95
GGLY96
GVAL135
GSER136
GASN137
GLEU164
GHIS192
GTHR247
GILE251
GOXM820
GHOH825
GHOH831

site_idCC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXM G 820
ChainResidue
GASN137
GLEU164
GARG168
GHIS192
GALA237
GNAI819

site_idCC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAI H 822
ChainResidue
HGLY28
HALA29
HVAL30
HASP51
HILE53
HTHR94
HALA95
HGLY96
HALA97
HARG98
HILE115
HVAL135
HASN137
HSER160
HLEU164
HHIS192
HTHR247
HILE251
HOXM823
HHOH830
HHOH847
HHOH864
HHOH873

site_idCC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OXM H 823
ChainResidue
HGLN99
HARG105
HASN137
HARG168
HHIS192
HALA237
HTHR247
HNAI822

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 Residues8
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues232
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11276087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues31
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
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 Residues24
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues24
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues24
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06151","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues16
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04642","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues8
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 Residues16
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS192
AASP165

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS192
BASP165
BARG168

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS192
CASP165
CARG168

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS192
DASP165
DARG168

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
EHIS192
EASP165
EARG168

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
FHIS192
FASP165
FARG168

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
GHIS192
GASP165
GARG168

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
HHIS192
HASP165
HARG168

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS192
BASP165

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS192
CASP165

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS192
DASP165

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
EHIS192
EASP165

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
FHIS192
FASP165

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
GHIS192
GASP165

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
HHIS192
HASP165

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS192
AASP165
AARG168

240971

PDB entries from 2025-08-27

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