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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1LDB

STRUCTURE DETERMINATION AND REFINEMENT OF BACILLUS STEAROTHERMOPHILUS LACTATE DEHYDROGENASE

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
A0051287molecular_functionNAD binding
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
B0051287molecular_functionNAD binding
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
C0051287molecular_functionNAD binding
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
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AARG169
AHIS193
AALA237
ATHR247
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AHIS186
ATYR188
DASN184
DHIS186
Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDT
ChainResidueDetails
AILE190-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":"PubMed","id":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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

246031

PDB entries from 2025-12-10

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