Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JML

Re-refined structure of R-state L-lactate dehydrogenase fromLactobacillus casei

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 PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue SO4 A 401

Chain	Residue
A	LEU153
A	ARG157
A	HIS181
A	ALA225
A	THR235
A	HOH502

site_id	AC2
Number of Residues	10
Details	binding site for residue SO4 A 402

Chain	Residue
A	HOH505
A	HOH520
B	SER172
B	HIS174
B	GLY195
B	HOH509
B	HOH530
A	ARG159
A	HIS174
A	TYR176

site_id	AC3
Number of Residues	7
Details	binding site for residue SO4 B 401

Chain	Residue
B	LEU153
B	ARG157
B	HIS181
B	ALA225
B	THR235
B	HOH523
B	HOH527

site_id	AC4
Number of Residues	9
Details	binding site for residue SO4 B 402

Chain	Residue
A	SER172
A	HIS174
A	GLY195
A	HOH539
B	ARG159
B	HIS174
B	TYR176
B	HOH520
B	HOH536

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 C 401

Chain	Residue
C	LEU153
C	ARG157
C	HIS181
C	ALA225
C	THR235

site_id	AC6
Number of Residues	10
Details	binding site for residue SO4 C 402

Chain	Residue
C	ARG159
C	HIS174
C	TYR176
C	HOH503
C	HOH509
C	HOH524
C	HOH530
F	SER172
F	HIS174
F	GLY195

site_id	AC7
Number of Residues	5
Details	binding site for residue SO4 D 401

Chain	Residue
D	LEU153
D	ARG157
D	HIS181
D	ALA225
D	THR235

site_id	AC8
Number of Residues	6
Details	binding site for residue SO4 D 402

Chain	Residue
D	ARG159
D	HIS174
D	TYR176
D	HOH501
E	HIS174
E	HOH509

site_id	AC9
Number of Residues	6
Details	binding site for residue SO4 E 401

Chain	Residue
E	ASN126
E	LEU153
E	ARG157
E	HIS181
E	ALA225
E	THR235

site_id	AD1
Number of Residues	10
Details	binding site for residue SO4 E 402

Chain	Residue
D	SER172
D	HIS174
D	GLY195
D	HOH503
E	ARG159
E	HIS174
E	TYR176
E	HOH504
E	HOH507
E	HOH508

site_id	AD2
Number of Residues	7
Details	binding site for residue SO4 F 401

Chain	Residue
F	LEU153
F	ARG157
F	HIS181
F	ALA225
F	THR235
F	HOH501
F	HOH504

site_id	AD3
Number of Residues	9
Details	binding site for residue SO4 F 402

Chain	Residue
C	HIS174
C	GLY195
C	HOH502
F	ARG159
F	HIS174
F	TYR176
F	HOH506
F	HOH509
F	HOH518

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

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

site_id	SWS_FT_FI2
Number of Residues	62
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
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

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