Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1T2F

Human B lactate dehydrogenase complexed with NAD+ and 4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004457	molecular_function	lactate dehydrogenase activity
A	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005829	cellular_component	cytosol
A	0006089	biological_process	lactate metabolic process
A	0016020	cellular_component	membrane
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	0019674	biological_process	NAD+ metabolic process
A	0019752	biological_process	carboxylic acid metabolic process
A	0019900	molecular_function	kinase binding
A	0042802	molecular_function	identical protein binding
A	0042867	biological_process	pyruvate catabolic process
A	0045121	cellular_component	membrane raft
A	0051287	molecular_function	NAD binding
A	0070062	cellular_component	extracellular exosome
A	1990204	cellular_component	oxidoreductase complex
B	0003824	molecular_function	catalytic activity
B	0004457	molecular_function	lactate dehydrogenase activity
B	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0005829	cellular_component	cytosol
B	0006089	biological_process	lactate metabolic process
B	0016020	cellular_component	membrane
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	0019674	biological_process	NAD+ metabolic process
B	0019752	biological_process	carboxylic acid metabolic process
B	0019900	molecular_function	kinase binding
B	0042802	molecular_function	identical protein binding
B	0042867	biological_process	pyruvate catabolic process
B	0045121	cellular_component	membrane raft
B	0051287	molecular_function	NAD binding
B	0070062	cellular_component	extracellular exosome
B	1990204	cellular_component	oxidoreductase complex
C	0003824	molecular_function	catalytic activity
C	0004457	molecular_function	lactate dehydrogenase activity
C	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0005829	cellular_component	cytosol
C	0006089	biological_process	lactate metabolic process
C	0016020	cellular_component	membrane
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	0019674	biological_process	NAD+ metabolic process
C	0019752	biological_process	carboxylic acid metabolic process
C	0019900	molecular_function	kinase binding
C	0042802	molecular_function	identical protein binding
C	0042867	biological_process	pyruvate catabolic process
C	0045121	cellular_component	membrane raft
C	0051287	molecular_function	NAD binding
C	0070062	cellular_component	extracellular exosome
C	1990204	cellular_component	oxidoreductase complex
D	0003824	molecular_function	catalytic activity
D	0004457	molecular_function	lactate dehydrogenase activity
D	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0005829	cellular_component	cytosol
D	0006089	biological_process	lactate metabolic process
D	0016020	cellular_component	membrane
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	0019674	biological_process	NAD+ metabolic process
D	0019752	biological_process	carboxylic acid metabolic process
D	0019900	molecular_function	kinase binding
D	0042802	molecular_function	identical protein binding
D	0042867	biological_process	pyruvate catabolic process
D	0045121	cellular_component	membrane raft
D	0051287	molecular_function	NAD binding
D	0070062	cellular_component	extracellular exosome
D	1990204	cellular_component	oxidoreductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD A 401

Chain	Residue
A	GLY29
A	VAL98
A	ARG99
A	VAL116
A	ILE120
A	VAL136
A	SER137
A	ASN138
A	SER161
A	HIS193
A	THR248
A	GLN30
A	ILE252
A	OXQ402
A	HOH433
A	HOH434
A	VAL31
A	ASP52
A	VAL53
A	LEU54
A	TYR83
A	THR95
A	GLY97

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OXQ A 402

Chain	Residue
A	GLN100
A	ARG106
A	ASN138
A	LEU165
A	ARG169
A	HIS193
A	THR248
A	NAD401

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD B 403

Chain	Residue
B	VAL28
B	GLY29
B	GLN30
B	VAL31
B	ASP52
B	VAL53
B	LEU54
B	THR95
B	ALA96
B	GLY97
B	VAL98
B	ARG99
B	GLN100
B	ILE120
B	VAL136
B	SER137
B	ASN138
B	SER161
B	HIS193
B	THR248
B	ILE252
B	OXQ404
B	HOH424
B	HOH473
B	HOH480
D	ASN108

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OXQ B 404

Chain	Residue
B	GLN100
B	ARG106
B	ASN138
B	ARG169
B	HIS193
B	THR248
B	NAD403
B	HOH480

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD C 405

Chain	Residue
A	ASN108
C	VAL28
C	GLY29
C	GLN30
C	VAL31
C	ASP52
C	VAL53
C	LEU54
C	THR95
C	ALA96
C	GLY97
C	VAL98
C	ARG99
C	VAL116
C	VAL136
C	ASN138
C	SER161
C	HIS193
C	THR248
C	ILE252
C	OXQ406
C	HOH419
C	HOH427
C	HOH437

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OXQ C 406

Chain	Residue
C	GLN100
C	ARG106
C	ASN138
C	LEU165
C	ARG169
C	HIS193
C	ALA238
C	THR248
C	NAD405
C	HOH419

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD D 407

Chain	Residue
D	GLY29
D	GLN30
D	VAL31
D	ASP52
D	VAL53
D	LEU54
D	THR95
D	ALA96
D	GLY97
D	VAL98
D	ARG99
D	VAL136
D	ASN138
D	SER161
D	LEU165
D	HIS193
D	THR248
D	ILE252
D	OXQ408
D	HOH419
D	HOH420
D	HOH443
D	HOH444

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OXQ D 408

Chain	Residue
D	GLN100
D	ARG106
D	ASN138
D	LEU165
D	ARG169
D	HIS193
D	ALA238
D	THR248
D	NAD407
D	HOH419

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	LEU190-SER196

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	88
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11276087","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

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	ASP166
A	HIS193

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

Chain	Residue	Details
B	ASP166
B	HIS193

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

Chain	Residue	Details
C	ASP166
C	HIS193

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

Chain	Residue	Details
D	ASP166
D	HIS193

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

Chain	Residue	Details
A	HIS193
A	ASP166
A	ARG169

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

Chain	Residue	Details
B	HIS193
B	ASP166
B	ARG169

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

Chain	Residue	Details
C	HIS193
C	ASP166
C	ARG169

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

Chain	Residue	Details
D	HIS193
D	ASP166
D	ARG169

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