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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2ZQY

T-state structure of allosteric L-lactate dehydrogenase from Lactobacillus casei

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006096biological_processglycolytic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0006089biological_processlactate metabolic process
B0006096biological_processglycolytic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
C0005737cellular_componentcytoplasm
C0006089biological_processlactate metabolic process
C0006096biological_processglycolytic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
D0003824molecular_functioncatalytic activity
D0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
D0005737cellular_componentcytoplasm
D0006089biological_processlactate metabolic process
D0006096biological_processglycolytic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 1
ChainResidue
AHIS186
AALA187
ATYR188
AHIS203
AASN205
site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 7
ChainResidue
DHIS186
DTYR188
DHOH367
ASER184
AHIS186
AGLY207
DARG171
site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 8
ChainResidue
AARG171
AHIS186
ATYR188
DSER184
DHIS186
DGLY207
site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 2
ChainResidue
BHIS186
BALA187
BTYR188
BHIS203
BHOH395
BHOH402
CGLY208
site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 5
ChainResidue
BARG171
BTYR188
BHOH356
BHOH402
CSER184
CHIS186
CGLY207
site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 6
ChainResidue
BSER184
BHIS186
BGLY207
BHOH404
CARG171
CTYR188
CHOH379
site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 C 3
ChainResidue
BGLY208
CHIS186
CALA187
CTYR188
CHIS203
CALA204
CHOH408
site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 D 4
ChainResidue
AGLY208
DHIS186
DALA187
DTYR188
DHIS203
DALA204
DHOH367
DHOH408
Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. MGEHGDT
ChainResidueDetails
AMET190-THR196
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"1984","firstPage":"32","lastPage":"34","volume":"40","journal":"Acta Crystallogr. A","title":"Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution.","authors":["Buehner M.","Hecht H.J."]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"1LLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASP166
AHIS193
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASP166
BHIS193
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CASP166
CHIS193
site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DASP166
DHIS193
site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS193
AASP166
AARG169
site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS193
BASP166
BARG169
site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS193
CASP166
CARG169
site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS193
DASP166
DARG169

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