6XXL
Crystal Structure of Human Deoxyhypusine Synthase in complex with spermine
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 | 0042802 | molecular_function | identical protein binding |
| A | 0046203 | biological_process | spermidine catabolic process |
| A | 0051604 | biological_process | protein maturation |
| 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 | 0042802 | molecular_function | identical protein binding |
| B | 0046203 | biological_process | spermidine catabolic process |
| B | 0051604 | biological_process | protein maturation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue FMT A 401 |
| Chain | Residue |
| A | LEU263 |
| A | ASN267 |
| A | HIS289 |
| A | ASN292 |
| A | ALA293 |
| B | THR237 |
| B | HOH628 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue SPM A 402 |
| Chain | Residue |
| A | ASP316 |
| A | GLU323 |
| A | TRP327 |
| A | LYS329 |
| A | HOH579 |
| B | ASN173 |
| B | SER240 |
| B | ASP243 |
| B | HOH503 |
| B | HOH547 |
| B | HOH596 |
| B | HOH681 |
| A | HIS288 |
| A | ASN292 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ASP313 |
| B | THR104 |
| B | ASN106 |
| B | GLY282 |
| B | ALA343 |
| B | HOH526 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | ASN106 |
| A | GLY282 |
| A | ALA343 |
| A | HOH530 |
| B | ASP313 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue OXM A 405 |
| Chain | Residue |
| A | CYS142 |
| A | LEU143 |
| A | ILE214 |
| A | ASN216 |
| A | HOH532 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue OXM A 406 |
| Chain | Residue |
| A | GLY50 |
| A | GLY60 |
| A | ARG61 |
| A | GLN64 |
| B | LEU148 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue ACT A 407 |
| Chain | Residue |
| B | TYR147 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 408 |
| Chain | Residue |
| A | GLU180 |
| A | PHE247 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 410 |
| Chain | Residue |
| A | LYS141 |
| A | CYS142 |
| A | ALA144 |
| A | PRO145 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue ACT A 411 |
| Chain | Residue |
| A | HOH570 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue ACT A 412 |
| Chain | Residue |
| A | HOH524 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue BME A 413 |
| Chain | Residue |
| A | LEU87 |
| A | GLN89 |
| A | GLU261 |
| A | ARG264 |
| A | LEU265 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 401 |
| Chain | Residue |
| A | PHE247 |
| B | ARG38 |
| B | GLY39 |
| B | VAL40 |
| B | HOH640 |
| site_id | AD5 |
| Number of Residues | 14 |
| Details | binding site for residue SPM B 402 |
| Chain | Residue |
| A | ASN173 |
| A | TYR176 |
| A | SER240 |
| A | ASP243 |
| A | HOH636 |
| A | HOH715 |
| B | HIS288 |
| B | ASN292 |
| B | ASP316 |
| B | GLU323 |
| B | TRP327 |
| B | LYS329 |
| B | HOH531 |
| B | HOH554 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | ALA208 |
| B | HIS228 |
| B | ILE229 |
| B | HOH502 |
| B | HOH511 |
| B | HOH696 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| A | VAL31 |
| A | ARG32 |
| B | ARG113 |
| B | GLU114 |
| B | GLU218 |
| B | HOH521 |
| B | HOH643 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 405 |
| Chain | Residue |
| B | TYR222 |
| B | HOH698 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9405486","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9493264","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 687 |
| Chain | Residue | Details |
| A | GLU137 | electrostatic stabiliser |
| A | ASN292 | proton acceptor, proton donor |
| A | ASP333 | 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 | ASN292 | proton acceptor, proton donor |
| B | ASP333 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
