Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2V6M

Crystal structure of lactate dehydrogenase from Thermus Thermophilus HB8 (Apo form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
A	0005737	cellular_component	cytoplasm
A	0006089	biological_process	lactate metabolic process
A	0006096	biological_process	glycolytic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019752	biological_process	carboxylic acid metabolic process
B	0003824	molecular_function	catalytic activity
B	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
B	0005737	cellular_component	cytoplasm
B	0006089	biological_process	lactate metabolic process
B	0006096	biological_process	glycolytic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0019752	biological_process	carboxylic acid metabolic process
C	0003824	molecular_function	catalytic activity
C	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
C	0005737	cellular_component	cytoplasm
C	0006089	biological_process	lactate metabolic process
C	0006096	biological_process	glycolytic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0019752	biological_process	carboxylic acid metabolic process
D	0003824	molecular_function	catalytic activity
D	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
D	0005737	cellular_component	cytoplasm
D	0006089	biological_process	lactate metabolic process
D	0006096	biological_process	glycolytic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0019752	biological_process	carboxylic acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MES D1332

Chain	Residue
C	PRO71
D	ARG256
D	TYR269
D	HOH1025
D	HOH1042
D	HOH1088

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MES B1332

Chain	Residue
B	ARG256
B	HOH1092
B	HOH1146
B	HOH1147
A	PRO71
A	PHE72
B	ALA170

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MES C1332

Chain	Residue
B	HOH1058
C	ARG256
D	PRO71
D	PHE72

Functional Information from PROSITE/UniProt

site_id	PS00064
Number of Residues	7
Details	L_LDH L-lactate dehydrogenase active site. LGEHGDS

Chain	Residue	Details
A	LEU192-SER198

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Structure of TT0471 protein from Thermus thermophilus.","authors":["Lokanath N.K.","Kunishima N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PubMed","id":"22319152","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2E37","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZZN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17936781","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Lactate dehydrogenase from T. thermophilus, penta-mutant (ternary complex with AMP).","authors":["Diop F.","Coquelle N.","Tickle J.","De Mendoza Barbera E.","Vellieux F.M.D."]}},{"source":"PDB","id":"2V7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XXJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
A	HIS195
A	ASP168

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
B	HIS195
B	ASP168

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
C	HIS195
C	ASP168

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
D	HIS195
D	ASP168

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
A	HIS195
A	ARG171
A	ASP168

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
B	HIS195
B	ARG171
B	ASP168

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
C	HIS195
C	ARG171
C	ASP168

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
D	HIS195
D	ARG171
D	ASP168

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)