Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2V7P

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004459	molecular_function	L-lactate dehydrogenase activity
A	0005737	cellular_component	cytoplasm
A	0006089	biological_process	lactate metabolic process
A	0006090	biological_process	pyruvate 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 activity
B	0005737	cellular_component	cytoplasm
B	0006089	biological_process	lactate metabolic process
B	0006090	biological_process	pyruvate 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 activity
C	0005737	cellular_component	cytoplasm
C	0006089	biological_process	lactate metabolic process
C	0006090	biological_process	pyruvate 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 activity
D	0005737	cellular_component	cytoplasm
D	0006089	biological_process	lactate metabolic process
D	0006090	biological_process	pyruvate 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	10
Details	BINDING SITE FOR RESIDUE OXM A 501

Chain	Residue
A	GLN102
A	HOH2146
A	ARG109
A	ASN140
A	LEU167
A	ARG171
A	HIS195
A	ALA236
A	THR246
A	NAD1332

site_id	AC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD A1332

Chain	Residue
A	GLY28
A	GLY30
A	MET31
A	VAL32
A	ASP53
A	LEU54
A	LEU58
A	TYR85
A	ALA98
A	GLY99
A	VAL100
A	ALA101
A	GLN102
A	VAL123
A	ALA138
A	THR139
A	ASN140
A	SER163
A	HIS195
A	THR246
A	ILE250
A	OXM501
A	HOH2072
A	HOH2110
A	HOH2142
A	HOH2143
A	HOH2144
A	HOH2145
A	HOH2146
A	HOH2147
C	GLN111
C	HOH2050

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXM B 501

Chain	Residue
B	ASN140
B	LEU167
B	ARG171
B	HIS195
B	ALA236
B	THR246
B	NAD1332
B	HOH2130
B	HOH2131

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD B1332

Chain	Residue
B	GLY30
B	MET31
B	VAL32
B	ASP53
B	LEU54
B	LEU58
B	ALA97
B	ALA98
B	VAL119
B	VAL123
B	ALA138
B	THR139
B	ASN140
B	SER163
B	LEU167
B	HIS195
B	THR246
B	ILE250
B	OXM501
B	HOH2031
B	HOH2053
B	HOH2100
B	HOH2130
B	HOH2132
B	HOH2133
B	HOH2135
B	HOH2136

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXM C 501

Chain	Residue
C	GLN102
C	ARG109
C	ASN140
C	LEU167
C	ARG171
C	HIS195
C	ALA236
C	THR246
C	NAD1332

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD C1332

Chain	Residue
C	ALA138
C	THR139
C	ASN140
C	SER163
C	HIS195
C	THR246
C	ILE250
C	OXM501
C	HOH2004
C	HOH2076
C	HOH2109
C	HOH2149
C	HOH2150
C	HOH2151
C	GLY30
C	MET31
C	VAL32
C	ASP53
C	LEU54
C	LEU58
C	TYR85
C	ALA98
C	GLY99
C	VAL100
C	ALA101
C	VAL123

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OXM D 501

Chain	Residue
D	ASN140
D	LEU167
D	ARG171
D	HIS195
D	ALA236
D	THR246
D	NAD1332

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD D1332

Chain	Residue
D	GLY30
D	MET31
D	VAL32
D	ASP53
D	LEU54
D	LEU58
D	TYR85
D	ALA97
D	ALA98
D	GLY99
D	VAL119
D	ALA138
D	THR139
D	ASN140
D	SER163
D	HIS195
D	THR246
D	ILE250
D	OXM501
D	HOH2030
D	HOH2098
D	HOH2099
D	HOH2100

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	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00488, ECO:0000305\|PubMed:17936781, ECO:0000305\|Ref.4, ECO:0007744\|PDB:2V7P, ECO:0007744\|PDB:2XXJ

Chain	Residue	Details
A	HIS195
B	HIS195
C	HIS195
D	HIS195

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00488, ECO:0000269\|PubMed:17936781, ECO:0000269\|Ref.2, ECO:0000269\|Ref.4, ECO:0000305\|PubMed:22319152, ECO:0007744\|PDB:2E37, ECO:0007744\|PDB:2V7P, ECO:0007744\|PDB:2XXB, ECO:0007744\|PDB:2XXJ, ECO:0007744\|PDB:3ZZN

Chain	Residue	Details
A	MET31
A	ASP53
A	GLY99
B	MET31
B	ASP53
B	GLY99
C	MET31
C	ASP53
C	GLY99
D	MET31
D	ASP53
D	GLY99

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00488, ECO:0000269\|PubMed:17936781, ECO:0000269\|Ref.4, ECO:0007744\|PDB:2V7P, ECO:0007744\|PDB:2XXB, ECO:0007744\|PDB:2XXJ

Chain	Residue	Details
A	TYR85
B	TYR85
C	TYR85
D	TYR85

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00488, ECO:0000305\|PubMed:17936781, ECO:0000305\|Ref.4, ECO:0007744\|PDB:2V7P, ECO:0007744\|PDB:2XXJ

Chain	Residue	Details
A	GLN102
A	ASP168
B	GLN102
B	ASP168
C	GLN102
C	ASP168
D	GLN102
D	ASP168

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:17936781, ECO:0000305\|Ref.4, ECO:0007744\|PDB:2V7P, ECO:0007744\|PDB:2XXJ

Chain	Residue	Details
A	ARG109
A	THR246
B	ARG108
B	THR246
C	ARG109
C	THR246
D	ARG108
D	THR246

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00488, ECO:0000269\|PubMed:17936781, ECO:0000269\|Ref.4, ECO:0007744\|PDB:2V7P, ECO:0007744\|PDB:2XXJ

Chain	Residue	Details
A	ALA138
B	ALA138
C	ALA138
D	ALA138

site_id	SWS_FT_FI7
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00488

Chain	Residue	Details
C	HIS188
D	ASN140
D	ARG173
D	HIS188
A	ASN140
A	ARG173
A	HIS188
B	ASN140
B	ARG173
B	HIS188
C	ASN140
C	ARG173

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:17936781, ECO:0000269\|Ref.4, ECO:0007744\|PDB:2V7P, ECO:0007744\|PDB:2XXJ

Chain	Residue	Details
A	SER163
B	SER163
C	SER163
D	SER163

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000255\|HAMAP-Rule:MF_00488

Chain	Residue	Details
A	TYR237
B	TYR237
C	TYR237
D	TYR237

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