Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ZQZ

R-state structure of allosteric L-lactate dehydrogenase from Lactobacillus 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 2

Chain	Residue
A	ARG169
A	HIS193
A	ALA237
A	THR247
A	HOH343
A	HOH381

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 7

Chain	Residue
A	HOH348
A	HOH376
B	SER184
B	HIS186
B	HOH352
B	HOH380
A	ARG171
A	HIS186
A	TYR188

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1

Chain	Residue
B	ARG169
B	HIS193
B	ALA237
B	THR247
B	HOH341
B	HOH356
B	HOH369

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 B 8

Chain	Residue
A	SER184
A	HIS186
A	GLY207
A	GLY208
A	HOH342
B	ARG171
B	HIS186
B	TYR188
B	HOH340
B	HOH342

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 3

Chain	Residue
C	LEU165
C	ARG169
C	HIS193
C	ALA237
C	THR247

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 C 9

Chain	Residue
C	ARG171
C	HIS186
C	TYR188
C	HOH341
C	HOH349
C	HOH361
F	SER184
F	HIS186
F	GLY207
F	GLY208
F	HOH360

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 5

Chain	Residue
D	LEU165
D	ARG169
D	HIS193
D	ALA237
D	THR247

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 11

Chain	Residue
D	ARG171
D	HIS186
D	TYR188
D	HOH347
D	HOH382
E	HIS186
E	HOH341

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 E 4

Chain	Residue
E	ASN138
E	LEU165
E	ARG169
E	HIS193
E	ALA237
E	THR247
E	HOH340
E	HOH374

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 E 10

Chain	Residue
D	SER184
D	HIS186
D	GLY207
D	HOH361
D	HOH375
E	ARG171
E	HIS186
E	TYR188
E	HOH343
E	HOH353
E	HOH379

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 F 6

Chain	Residue
F	LEU165
F	ARG169
F	HIS193
F	ALA237
F	THR247
F	HOH340
F	HOH353
F	HOH355

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 F 339

Chain	Residue
C	SER184
C	HIS186
C	GLY207
C	GLY208
F	ARG171
F	HIS186
F	TYR188
F	HOH341
F	HOH349
F	HOH362
F	HOH376

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	MET190-THR196

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

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	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
D	HIS193
D	ASP166
D	ARG169

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
E	HIS193
E	ASP166
E	ARG169

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
F	HIS193
F	ASP166
F	ARG169

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	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
E	ASP166
E	HIS193

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
F	ASP166
F	HIS193

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
A	HIS193
A	ASP166
A	ARG169

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
B	HIS193
B	ASP166
B	ARG169

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1emd

Chain	Residue	Details
C	HIS193
C	ASP166
C	ARG169

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