1LDN
STRUCTURE OF A TERNARY COMPLEX OF AN ALLOSTERIC LACTATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006089 | biological_process | lactate metabolic process |
A | 0006090 | biological_process | pyruvate 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 activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006089 | biological_process | lactate metabolic process |
B | 0006090 | biological_process | pyruvate 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 activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006089 | biological_process | lactate metabolic process |
C | 0006090 | biological_process | pyruvate 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 activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006089 | biological_process | lactate metabolic process |
D | 0006090 | biological_process | pyruvate 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 |
E | 0003824 | molecular_function | catalytic activity |
E | 0004459 | molecular_function | L-lactate dehydrogenase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0006089 | biological_process | lactate metabolic process |
E | 0006090 | biological_process | pyruvate 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 | 0051287 | molecular_function | NAD binding |
F | 0003824 | molecular_function | catalytic activity |
F | 0004459 | molecular_function | L-lactate dehydrogenase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006089 | biological_process | lactate metabolic process |
F | 0006090 | biological_process | pyruvate 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 | 0051287 | molecular_function | NAD binding |
G | 0003824 | molecular_function | catalytic activity |
G | 0004459 | molecular_function | L-lactate dehydrogenase activity |
G | 0005737 | cellular_component | cytoplasm |
G | 0006089 | biological_process | lactate metabolic process |
G | 0006090 | biological_process | pyruvate 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 | 0051287 | molecular_function | NAD binding |
H | 0003824 | molecular_function | catalytic activity |
H | 0004459 | molecular_function | L-lactate dehydrogenase activity |
H | 0005737 | cellular_component | cytoplasm |
H | 0006089 | biological_process | lactate metabolic process |
H | 0006090 | biological_process | pyruvate 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 | 0051287 | molecular_function | NAD binding |
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 | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN |
Chain | Residue | Details |
A | HIS193 | |
B | HIS193 | |
C | HIS193 | |
D | HIS193 | |
E | HIS193 | |
F | HIS193 | |
G | HIS193 | |
H | HIS193 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB |
Chain | Residue | Details |
A | PHE30 | |
D | PHE30 | |
D | ASP52 | |
D | ALA136 | |
E | PHE30 | |
E | ASP52 | |
E | ALA136 | |
F | PHE30 | |
F | ASP52 | |
F | ALA136 | |
G | PHE30 | |
A | ASP52 | |
G | ASP52 | |
G | ALA136 | |
H | PHE30 | |
H | ASP52 | |
H | ALA136 | |
A | ALA136 | |
B | PHE30 | |
B | ASP52 | |
B | ALA136 | |
C | PHE30 | |
C | ASP52 | |
C | ALA136 |
site_id | SWS_FT_FI3 |
Number of Residues | 48 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | LYS57 | |
B | GLN100 | |
B | SER119 | |
B | ASN138 | |
C | LYS57 | |
C | TYR83 | |
C | GLY97 | |
C | GLN100 | |
C | SER119 | |
C | ASN138 | |
D | LYS57 | |
A | TYR83 | |
D | TYR83 | |
D | GLY97 | |
D | GLN100 | |
D | SER119 | |
D | ASN138 | |
E | LYS57 | |
E | TYR83 | |
E | GLY97 | |
E | GLN100 | |
E | SER119 | |
A | GLY97 | |
E | ASN138 | |
F | LYS57 | |
F | TYR83 | |
F | GLY97 | |
F | GLN100 | |
F | SER119 | |
F | ASN138 | |
G | LYS57 | |
G | TYR83 | |
G | GLY97 | |
A | GLN100 | |
G | GLN100 | |
G | SER119 | |
G | ASN138 | |
H | LYS57 | |
H | TYR83 | |
H | GLY97 | |
H | GLN100 | |
H | SER119 | |
H | ASN138 | |
A | SER119 | |
A | ASN138 | |
B | LYS57 | |
B | TYR83 | |
B | GLY97 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN |
Chain | Residue | Details |
A | ARG106 | |
D | ARG106 | |
D | ASP166 | |
D | THR247 | |
E | ARG106 | |
E | ASP166 | |
E | THR247 | |
F | ARG106 | |
F | ASP166 | |
F | THR247 | |
G | ARG106 | |
A | ASP166 | |
G | ASP166 | |
G | THR247 | |
H | ARG106 | |
H | ASP166 | |
H | THR247 | |
A | THR247 | |
B | ARG106 | |
B | ASP166 | |
B | THR247 | |
C | ARG106 | |
C | ASP166 | |
C | THR247 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB |
Chain | Residue | Details |
A | SER161 | |
E | GLN183 | |
F | SER161 | |
F | GLN183 | |
G | SER161 | |
G | GLN183 | |
H | SER161 | |
H | GLN183 | |
A | GLN183 | |
B | SER161 | |
B | GLN183 | |
C | SER161 | |
C | GLN183 | |
D | SER161 | |
D | GLN183 | |
E | SER161 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:2LDB |
Chain | Residue | Details |
A | ARG171 | |
B | ARG171 | |
C | ARG171 | |
D | ARG171 | |
E | ARG171 | |
F | ARG171 | |
G | ARG171 | |
H | ARG171 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | TYR238 | |
B | TYR238 | |
C | TYR238 | |
D | TYR238 | |
E | TYR238 | |
F | TYR238 | |
G | TYR238 | |
H | TYR238 |
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 |
B | HIS193 | |
B | ASP166 | |
B | ARG169 |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
C | HIS193 | |
C | ASP166 | |
C | ARG169 |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
D | HIS193 | |
D | ASP166 | |
D | ARG169 |
site_id | CSA13 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
E | HIS193 | |
E | ASP166 | |
E | ARG169 |
site_id | CSA14 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
F | HIS193 | |
F | ASP166 | |
F | ARG169 |
site_id | CSA15 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
G | HIS193 | |
G | ASP166 | |
G | ARG169 |
site_id | CSA16 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
H | HIS193 | |
H | ASP166 | |
H | 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 | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
G | ASP166 | |
G | HIS193 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
H | ASP166 | |
H | HIS193 |
site_id | CSA9 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | HIS193 | |
A | ASP166 | |
A | ARG169 |