2E37
Structure of TT0471 protein from Thermus thermophilus
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 | 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 activity |
B | 0005737 | cellular_component | cytoplasm |
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 activity |
C | 0005737 | cellular_component | cytoplasm |
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 activity |
D | 0005737 | cellular_component | cytoplasm |
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 activity |
E | 0005737 | cellular_component | cytoplasm |
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 activity |
F | 0005737 | cellular_component | cytoplasm |
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 |
G | 0003824 | molecular_function | catalytic activity |
G | 0004459 | molecular_function | L-lactate dehydrogenase activity |
G | 0005737 | cellular_component | cytoplasm |
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 |
H | 0003824 | molecular_function | catalytic activity |
H | 0004459 | molecular_function | L-lactate dehydrogenase activity |
H | 0005737 | cellular_component | cytoplasm |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1501 |
Chain | Residue |
B | VAL6 |
B | GLY7 |
B | ASP32 |
B | LEU33 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 H 1502 |
Chain | Residue |
H | ASP32 |
H | LEU33 |
H | TYR62 |
H | ALA75 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAD A 1401 |
Chain | Residue |
A | GLY9 |
A | MSE10 |
A | VAL11 |
A | ASP32 |
A | LEU33 |
A | LEU37 |
A | ALA74 |
A | ALA75 |
A | GLY76 |
A | VAL77 |
A | ASN92 |
A | THR116 |
A | ASN117 |
A | ILE221 |
A | ALA226 |
A | THR227 |
A | HOH1411 |
A | SER8 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAD C 1402 |
Chain | Residue |
C | GLY7 |
C | SER8 |
C | GLY9 |
C | MSE10 |
C | VAL11 |
C | ASP32 |
C | LEU33 |
C | LEU37 |
C | ALA75 |
C | GLY76 |
C | VAL77 |
C | ASN92 |
C | VAL95 |
C | ASN117 |
C | ILE221 |
C | ALA226 |
C | THR227 |
C | HOH1479 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAD E 1403 |
Chain | Residue |
E | SER8 |
E | GLY9 |
E | MSE10 |
E | VAL11 |
E | ASP32 |
E | LEU33 |
E | LEU37 |
E | ALA75 |
E | GLY76 |
E | VAL77 |
E | ASN92 |
E | ASN117 |
E | ILE221 |
E | ALA226 |
E | THR227 |
E | HOH1410 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAD G 1404 |
Chain | Residue |
G | SER8 |
G | GLY9 |
G | MSE10 |
G | VAL11 |
G | ASP32 |
G | LEU33 |
G | LEU37 |
G | ALA75 |
G | GLY76 |
G | VAL77 |
G | ASN92 |
G | VAL95 |
G | ASN117 |
G | ILE221 |
G | ALA226 |
G | THR227 |
G | HOH1437 |
G | HOH1480 |
Functional Information from PROSITE/UniProt
site_id | PS00064 |
Number of Residues | 7 |
Details | L_LDH L-lactate dehydrogenase active site. LGEHGDS |
Chain | Residue | Details |
A | LEU169-SER175 |
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:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
Chain | Residue | Details |
A | HIS172 | |
B | HIS172 | |
C | HIS172 | |
D | HIS172 | |
E | HIS172 | |
F | HIS172 | |
G | HIS172 | |
H | HIS172 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.2, ECO:0000269|Ref.4, ECO:0000305|PubMed:22319152, ECO:0007744|PDB:2E37, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ, ECO:0007744|PDB:3ZZN |
Chain | Residue | Details |
A | MSE10 | |
D | MSE10 | |
D | ASP32 | |
D | GLY76 | |
E | MSE10 | |
E | ASP32 | |
E | GLY76 | |
F | MSE10 | |
F | ASP32 | |
F | GLY76 | |
G | MSE10 | |
A | ASP32 | |
G | ASP32 | |
G | GLY76 | |
H | MSE10 | |
H | ASP32 | |
H | GLY76 | |
A | GLY76 | |
B | MSE10 | |
B | ASP32 | |
B | GLY76 | |
C | MSE10 | |
C | ASP32 | |
C | GLY76 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXB, ECO:0007744|PDB:2XXJ |
Chain | Residue | Details |
A | TYR62 | |
B | TYR62 | |
C | TYR62 | |
D | TYR62 | |
E | TYR62 | |
F | TYR62 | |
G | TYR62 | |
H | TYR62 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
Chain | Residue | Details |
A | GLN79 | |
E | ASP145 | |
F | GLN79 | |
F | ASP145 | |
G | GLN79 | |
G | ASP145 | |
H | GLN79 | |
H | ASP145 | |
A | ASP145 | |
B | GLN79 | |
B | ASP145 | |
C | GLN79 | |
C | ASP145 | |
D | GLN79 | |
D | ASP145 | |
E | GLN79 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000305|PubMed:17936781, ECO:0000305|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
Chain | Residue | Details |
A | ARG85 | |
E | THR227 | |
F | ARG85 | |
F | THR227 | |
G | ARG85 | |
G | THR227 | |
H | ARG85 | |
H | THR227 | |
A | THR227 | |
B | ARG85 | |
B | THR227 | |
C | ARG85 | |
C | THR227 | |
D | ARG85 | |
D | THR227 | |
E | ARG85 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
Chain | Residue | Details |
A | ALA115 | |
B | ALA115 | |
C | ALA115 | |
D | ALA115 | |
E | ALA115 | |
F | ALA115 | |
G | ALA115 | |
H | ALA115 |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | ASN117 | |
D | ASN117 | |
D | ARG150 | |
D | HIS165 | |
E | ASN117 | |
E | ARG150 | |
E | HIS165 | |
F | ASN117 | |
F | ARG150 | |
F | HIS165 | |
G | ASN117 | |
A | ARG150 | |
G | ARG150 | |
G | HIS165 | |
H | ASN117 | |
H | ARG150 | |
H | HIS165 | |
A | HIS165 | |
B | ASN117 | |
B | ARG150 | |
B | HIS165 | |
C | ASN117 | |
C | ARG150 | |
C | HIS165 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17936781, ECO:0000269|Ref.4, ECO:0007744|PDB:2V7P, ECO:0007744|PDB:2XXJ |
Chain | Residue | Details |
A | SER140 | |
B | SER140 | |
C | SER140 | |
D | SER140 | |
E | SER140 | |
F | SER140 | |
G | SER140 | |
H | SER140 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488 |
Chain | Residue | Details |
A | TYR218 | |
B | TYR218 | |
C | TYR218 | |
D | TYR218 | |
E | TYR218 | |
F | TYR218 | |
G | TYR218 | |
H | TYR218 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | HIS172 | |
A | ASP145 |
site_id | CSA10 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | HIS172 | |
B | ASP145 | |
B | ARG148 |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
C | HIS172 | |
C | ASP145 | |
C | ARG148 |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
D | HIS172 | |
D | ASP145 | |
D | ARG148 |
site_id | CSA13 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
E | HIS172 | |
E | ASP145 | |
E | ARG148 |
site_id | CSA14 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
F | HIS172 | |
F | ASP145 | |
F | ARG148 |
site_id | CSA15 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
G | HIS172 | |
G | ASP145 | |
G | ARG148 |
site_id | CSA16 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
H | HIS172 | |
H | ASP145 | |
H | ARG148 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
B | HIS172 | |
B | ASP145 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
C | HIS172 | |
C | ASP145 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
D | HIS172 | |
D | ASP145 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
E | HIS172 | |
E | ASP145 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
F | HIS172 | |
F | ASP145 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
G | HIS172 | |
G | ASP145 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
H | HIS172 | |
H | ASP145 |
site_id | CSA9 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1emd |
Chain | Residue | Details |
A | HIS172 | |
A | ASP145 | |
A | ARG148 |