1RQD
deoxyhypusine synthase holoenzyme in its low ionic strength, high pH crystal form with the inhibitor GC7 bound in the active site
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 | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 370 |
| Chain | Residue |
| A | THR104 |
| A | GLY282 |
| A | GLY283 |
| A | ILE306 |
| A | ASN307 |
| A | THR308 |
| A | ALA309 |
| A | ALA341 |
| A | ASP342 |
| A | ALA343 |
| B | GLY284 |
| A | SER105 |
| B | HIS288 |
| B | ASP313 |
| B | SER315 |
| B | ASP316 |
| B | SER317 |
| B | NAD370 |
| B | GC7371 |
| A | ASN106 |
| A | SER109 |
| A | THR131 |
| A | ALA132 |
| A | GLY133 |
| A | GLU137 |
| A | ASP238 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD B 370 |
| Chain | Residue |
| A | GLY284 |
| A | VAL285 |
| A | HIS288 |
| A | ASP313 |
| A | SER315 |
| A | ASP316 |
| A | SER317 |
| A | NAD370 |
| A | GC7371 |
| B | THR104 |
| B | SER105 |
| B | ASN106 |
| B | LEU107 |
| B | SER109 |
| B | THR131 |
| B | ALA132 |
| B | GLY133 |
| B | GLU137 |
| B | ASP238 |
| B | GLY282 |
| B | GLY283 |
| B | ASN307 |
| B | THR308 |
| B | ALA309 |
| B | ALA341 |
| B | ASP342 |
| B | ALA343 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GC7 A 371 |
| Chain | Residue |
| A | HIS288 |
| A | ASN292 |
| A | LEU295 |
| A | GLY314 |
| A | SER315 |
| A | ASP316 |
| A | GLU323 |
| A | TRP327 |
| A | LYS329 |
| B | ASP243 |
| B | NAD370 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GC7 B 371 |
| Chain | Residue |
| A | ILE166 |
| A | GLY167 |
| A | ASP243 |
| A | NAD370 |
| B | HIS288 |
| B | ASN292 |
| B | GLY314 |
| B | SER315 |
| B | ASP316 |
| B | GLU323 |
| B | TRP327 |
| B | LYS329 |
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 | GLU137 | |
| A | ASP238 | |
| A | GLY283 | |
| A | THR308 | |
| A | ASP342 | |
| B | SER105 | |
| B | THR131 | |
| B | GLU137 | |
| B | ASP238 | |
| B | GLY283 | |
| B | THR308 | |
| B | ASP342 | |
| A | SER105 | |
| A | THR131 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU323 | |
| B | GLU136 | |
| B | ASP243 | |
| B | HIS288 | |
| B | GLY314 | |
| B | GLU323 | |
| A | GLU136 | |
| A | ASP243 | |
| A | HIS288 | |
| A | 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 |
