6WKZ
Cocomplex structure of Deoxyhypusine synthase with inhibitor 6-[(1R)-2-AMINO-1-PHENYLETHYL]-3-(PYRIDIN-3-YL)-4H,5H,6H,7H-THIENO[2,3-C]PYRIDIN-7-ONE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006412 | biological_process | translation |
A | 0008216 | biological_process | spermidine metabolic process |
A | 0008284 | biological_process | positive regulation of cell population proliferation |
A | 0008612 | biological_process | peptidyl-lysine modification to peptidyl-hypusine |
A | 0016740 | molecular_function | transferase activity |
A | 0034038 | molecular_function | deoxyhypusine synthase activity |
A | 0042102 | biological_process | positive regulation of T cell proliferation |
A | 0042593 | biological_process | glucose homeostasis |
A | 0042802 | molecular_function | identical protein binding |
A | 0046203 | biological_process | spermidine catabolic process |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006412 | biological_process | translation |
B | 0008216 | biological_process | spermidine metabolic process |
B | 0008284 | biological_process | positive regulation of cell population proliferation |
B | 0008612 | biological_process | peptidyl-lysine modification to peptidyl-hypusine |
B | 0016740 | molecular_function | transferase activity |
B | 0034038 | molecular_function | deoxyhypusine synthase activity |
B | 0042102 | biological_process | positive regulation of T cell proliferation |
B | 0042593 | biological_process | glucose homeostasis |
B | 0042802 | molecular_function | identical protein binding |
B | 0046203 | biological_process | spermidine catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 8Y1 A 701 |
Chain | Residue |
A | THR237 |
B | ALA270 |
B | VAL286 |
B | LYS287 |
B | HOH832 |
A | ASP238 |
A | ASP243 |
B | PHE100 |
B | PRO234 |
B | ILE259 |
B | ASP262 |
B | LEU263 |
B | ASN267 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue 8Y1 B 701 |
Chain | Residue |
A | PRO234 |
A | ILE259 |
A | ASP262 |
A | LEU263 |
A | ASN267 |
A | ALA270 |
A | VAL285 |
A | VAL286 |
A | LYS287 |
A | HOH825 |
B | THR237 |
B | ASP238 |
B | ASP243 |
B | HOH821 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:9405486 |
Chain | Residue | Details |
A | LYS329 | |
B | LYS329 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9493264 |
Chain | Residue | Details |
A | SER105 | |
B | GLU137 | |
B | ASP238 | |
B | GLY283 | |
B | THR308 | |
B | ASP342 | |
A | THR131 | |
A | GLU137 | |
A | ASP238 | |
A | GLY283 | |
A | THR308 | |
A | ASP342 | |
B | SER105 | |
B | THR131 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | GLU136 | |
B | GLU323 | |
A | ASP243 | |
A | HIS288 | |
A | GLY314 | |
A | GLU323 | |
B | GLU136 | |
B | ASP243 | |
B | HIS288 | |
B | GLY314 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER78 | |
B | SER78 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 687 |
Chain | Residue | Details |
A | GLU137 | electrostatic stabiliser |
A | HIS288 | proton acceptor, proton donor |
A | LYS329 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 687 |
Chain | Residue | Details |
B | GLU137 | electrostatic stabiliser |
B | HIS288 | proton acceptor, proton donor |
B | LYS329 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |