6XXH
Crystal Structure of Human Deoxyhypusine Synthase in apo form
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 | 5 |
| Details | binding site for residue BME A 401 |
| Chain | Residue |
| A | ASN173 |
| A | TYR176 |
| A | CSS177 |
| A | GLU180 |
| A | MET244 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MRD B 401 |
| Chain | Residue |
| B | HOH668 |
| A | PHE247 |
| A | TYR250 |
| B | ARG38 |
| B | VAL40 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 402 |
| Chain | Residue |
| A | SER28 |
| B | ILE163 |
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 |
