1EZ4

CRYSTAL STRUCTURE OF NON-ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS PENTOSUS AT 2.3 ANGSTROM RESOLUTION

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	22
Details	BINDING SITE FOR RESIDUE NAD A 1352

Chain	Residue
A	GLY29
A	GLY97
A	ALA98
A	ILE116
A	SER119
A	ALA136
A	ASN138
A	VAL140
A	SER161
A	LEU165
A	HIS193
A	ALA30
A	HOH1427
A	HOH1476
A	HOH1527
A	VAL31
A	ASP52
A	VAL53
A	ARG57
A	TYR83
A	THR95
A	ALA96

---

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD B 1353

Chain	Residue
B	ASP28
B	GLY29
B	ALA30
B	VAL31
B	ASP52
B	VAL54
B	THR95
B	ALA96
B	GLY97
B	ILE116
B	ALA136
B	ALA137
B	ASN138
B	VAL140
B	SER161
B	LEU165
B	HIS193
B	ILE251
B	HOH1457
B	HOH1458
B	HOH1471
B	HOH1472
B	HOH1544
B	HOH1557

---

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD C 1354

Chain	Residue
C	ASP28
C	GLY29
C	ALA30
C	VAL31
C	ASP52
C	VAL53
C	ARG57
C	TYR83
C	THR95
C	ALA96
C	GLY97
C	ILE116
C	SER119
C	ALA136
C	ASN138
C	VAL140
C	SER161
C	HIS193
C	ILE251
C	HOH1429
C	HOH1528

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD D 1355

Chain	Residue
D	GLY29
D	ALA30
D	VAL31
D	ASP52
D	VAL53
D	THR95
D	ALA96
D	GLY97
D	ILE116
D	SER119
D	ALA136
D	ALA137
D	ASN138
D	SER161
D	LEU165
D	HIS193
D	ILE251
D	HOH1387
D	HOH1452
D	HOH1467
D	HOH1468

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET190-SER196

---

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":"11807949","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1425707","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1EZ4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11807949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EZ4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
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	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

---