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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3PQF

Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+

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
A0042867biological_processpyruvate catabolic 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
B0042867biological_processpyruvate catabolic 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
C0042867biological_processpyruvate catabolic 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
D0042867biological_processpyruvate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAD C 352
ChainResidue
CILE11
CGLY82
CALA83
CTHR122
CTHR232
CHOH332
CGLY14
CPHE15
CVAL16
CASP37
CVAL38
CTYR68
CCYS80
CALA81
site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAD D 352
ChainResidue
DGLY14
DPHE15
DVAL16
DASP37
DVAL38
DTYR68
DCYS80
DALA81
DGLY82
DALA83
DILE101
DTHR122
DTHR232
DHOH327
Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDT
ChainResidueDetails
AILE175-THR181
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":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PQF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","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":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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