3ZZN

5-Mutant (R79W, R151A, E279A, E299A,E313A) Lactate-Dehydrogenase from Thermus thermophillus

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	17
Details	BINDING SITE FOR RESIDUE ADP A 1332

Chain	Residue
A	GLY30
A	GLY99
A	VAL123
A	HOH2004
A	HOH2117
A	HOH2119
B	GLY106
B	GLU107
B	GLN111
A	MET31
A	VAL32
A	ASP53
A	LEU54
A	LEU58
A	TYR85
A	ALA97
A	ALA98

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP D 1332

Chain	Residue
C	GLY106
C	GLN111
D	GLY30
D	MET31
D	VAL32
D	ASP53
D	LEU54
D	LEU58
D	TYR85
D	ALA97
D	ALA98
D	GLY99
D	VAL119
D	HOH2077
D	HOH2078

---

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
D	MET31
D	ASP53
D	GLY99
A	ASP53
A	GLY99
B	MET31
B	ASP53
B	GLY99
C	MET31
C	ASP53
C	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	ARG109
B	THR246
C	ARG109
C	THR246
D	ARG109
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
A	ASN140
D	ASN140
D	ARG173
D	HIS188
A	ARG173
A	HIS188
B	ASN140
B	ARG173
B	HIS188
C	ASN140
C	ARG173
C	HIS188

---

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

---