6J9T

Complex structure of Lactobacillus casei lactate dehydrogenase with fructose-1,6-bisphosphate

Replaces:  3VKV

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
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
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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET178-THR184

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"1984","firstPage":"32","lastPage":"34","volume":"40","journal":"Acta Crystallogr. A","title":"Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution.","authors":["Buehner M.","Hecht H.J."]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"1LLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	66
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of penta mutant of L-lactate dehydrogenase from Lactobacillus casei.","authors":["Arai K.","Miyanaga A.","Uchikoba H.","Fushinobu S.","Taguchi H."]}},{"source":"PDB","id":"6J9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J9U","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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