3PQD

Crystal structure of L-lactate dehydrogenase from Bacillus subtilis complexed with FBP and NAD+

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
A	0042867	biological_process	pyruvate catabolic 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
B	0042867	biological_process	pyruvate catabolic 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
C	0042867	biological_process	pyruvate catabolic 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
D	0042867	biological_process	pyruvate catabolic process
E	0003824	molecular_function	catalytic activity
E	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
E	0005737	cellular_component	cytoplasm
E	0006089	biological_process	lactate metabolic process
E	0006096	biological_process	glycolytic process
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0019752	biological_process	carboxylic acid metabolic process
E	0042867	biological_process	pyruvate catabolic process
F	0003824	molecular_function	catalytic activity
F	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
F	0005737	cellular_component	cytoplasm
F	0006089	biological_process	lactate metabolic process
F	0006096	biological_process	glycolytic process
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0019752	biological_process	carboxylic acid metabolic process
F	0042867	biological_process	pyruvate catabolic process
G	0003824	molecular_function	catalytic activity
G	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
G	0005737	cellular_component	cytoplasm
G	0006089	biological_process	lactate metabolic process
G	0006096	biological_process	glycolytic process
G	0016491	molecular_function	oxidoreductase activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0019752	biological_process	carboxylic acid metabolic process
G	0042867	biological_process	pyruvate catabolic process
H	0003824	molecular_function	catalytic activity
H	0004459	molecular_function	L-lactate dehydrogenase (NAD+) activity
H	0005737	cellular_component	cytoplasm
H	0006089	biological_process	lactate metabolic process
H	0006096	biological_process	glycolytic process
H	0016491	molecular_function	oxidoreductase activity
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0019752	biological_process	carboxylic acid metabolic process
H	0042867	biological_process	pyruvate catabolic process

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE175-THR181

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PQF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	89
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","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":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of L-lactate dehydrogenase from Bacillus subtilis mutation H171C complexed with NAD+.","authors":["Zhang Y.","Garavito R.M."]}},{"source":"PDB","id":"3PQD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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