Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2LDB

STRUCTURE DETERMINATION AND REFINEMENT OF BACILLUS STEAROTHERMOPHILUS LACTATE DEHYDROGENASE

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	0051287	molecular_function	NAD binding
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	0051287	molecular_function	NAD binding
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	0051287	molecular_function	NAD binding
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	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	FBA
Number of Residues	10
Details	FBP binding site

Chain	Residue
A	ARG171
A	PRO182
A	GLN183
A	ASN184
A	VAL185
A	HIS186
A	ALA187
A	TYR188
A	GLY207
A	ILE269

site_id	FBB
Number of Residues	10
Details	FBP binding site

Chain	Residue
B	ARG171
B	PRO182
B	GLN183
B	ASN184
B	VAL185
B	HIS186
B	ALA187
B	TYR188
B	GLY207
B	ILE269

site_id	FBC
Number of Residues	10
Details	FBP binding site

Chain	Residue
C	VAL185
C	HIS186
C	ALA187
C	TYR188
C	GLY207
C	ILE269
C	ARG171
C	PRO182
C	GLN183
C	ASN184

site_id	FBD
Number of Residues	10
Details	FBP binding site

Chain	Residue
D	ARG171
D	PRO182
D	GLN183
D	ASN184
D	VAL185
D	HIS186
D	ALA187
D	TYR188
D	GLY207
D	ILE269

site_id	NAA
Number of Residues	25
Details	NAD binding site

Chain	Residue
A	ILE26
A	ALA53
A	ASN54
A	LYS57
A	TYR83
A	CYS95
A	ALA96
A	GLY97
A	ALA98
A	ILE116
A	ILE120
A	GLY27
A	ALA136
A	THR137
A	ASN138
A	SER161
A	LEU165
A	HIS193
A	ALA28
A	GLY29
A	PHE30
A	VAL31
A	GLY32
A	ILE51
A	ASP52

site_id	NAB
Number of Residues	25
Details	NAD binding site

Chain	Residue
B	ILE26
B	GLY27
B	ALA28
B	GLY29
B	PHE30
B	VAL31
B	GLY32
B	ILE51
B	ASP52
B	ALA53
B	ASN54
B	LYS57
B	TYR83
B	CYS95
B	ALA96
B	GLY97
B	ALA98
B	ILE116
B	ILE120
B	ALA136
B	THR137
B	ASN138
B	SER161
B	LEU165
B	HIS193

site_id	NAC
Number of Residues	25
Details	NAD binding site

Chain	Residue
C	ILE26
C	GLY27
C	ALA28
C	GLY29
C	PHE30
C	VAL31
C	GLY32
C	ILE51
C	ASP52
C	ALA53
C	ASN54
C	LYS57
C	TYR83
C	CYS95
C	ALA96
C	GLY97
C	ALA98
C	ILE116
C	ILE120
C	ALA136
C	THR137
C	ASN138
C	SER161
C	LEU165
C	HIS193

site_id	NAD
Number of Residues	25
Details	NAD binding site

Chain	Residue
D	ILE26
D	GLY27
D	ALA28
D	GLY29
D	PHE30
D	VAL31
D	GLY32
D	ILE51
D	ASP52
D	ALA53
D	ASN54
D	LYS57
D	TYR83
D	CYS95
D	ALA96
D	GLY97
D	ALA98
D	ILE116
D	ILE120
D	ALA136
D	THR137
D	ASN138
D	SER161
D	LEU165
D	HIS193

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	ILE190-THR196

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":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]}

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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"1731077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]}

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":"PubMed","id":"1731077","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1LDN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00488","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2330370","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2LDB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)