3LJU
Crystal structure of full length centaurin alpha-1 bound with the head group of PIP3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0005096 | molecular_function | GTPase activator activity |
| X | 0005515 | molecular_function | protein binding |
| X | 0005547 | molecular_function | phosphatidylinositol-3,4,5-trisphosphate binding |
| X | 0005634 | cellular_component | nucleus |
| X | 0005737 | cellular_component | cytoplasm |
| X | 0005829 | cellular_component | cytosol |
| X | 0005886 | cellular_component | plasma membrane |
| X | 0007166 | biological_process | cell surface receptor signaling pathway |
| X | 0008270 | molecular_function | zinc ion binding |
| X | 0043087 | biological_process | regulation of GTPase activity |
| X | 0043533 | molecular_function | inositol 1,3,4,5 tetrakisphosphate binding |
| X | 0043547 | biological_process | positive regulation of GTPase activity |
| X | 0046872 | molecular_function | metal ion binding |
| X | 1902936 | molecular_function | phosphatidylinositol bisphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN X 401 |
| Chain | Residue |
| X | CYS21 |
| X | CYS24 |
| X | CYS41 |
| X | CYS44 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE IP9 X 371 |
| Chain | Residue |
| X | GLU268 |
| X | ARG271 |
| X | ARG273 |
| X | TYR284 |
| X | ARG332 |
| X | HOH463 |
| X | HOH470 |
| X | HOH498 |
| X | HOH541 |
| X | HOH573 |
| X | HOH580 |
| X | HOH603 |
| X | SER43 |
| X | LYS261 |
| X | THR262 |
| X | GLY263 |
| X | PRO264 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE IP9 X 372 |
| Chain | Residue |
| X | LYS138 |
| X | GLY140 |
| X | ARG141 |
| X | ARG149 |
| X | TYR162 |
| X | ASN164 |
| X | LYS172 |
| X | ARG206 |
| X | THR340 |
| X | GLU341 |
| X | SER342 |
| X | ARG345 |
| X | HOH423 |
| X | HOH442 |
| X | HOH471 |
| X | HOH506 |
| X | HOH531 |
| X | HOH637 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 119 |
| Details | Domain: {"description":"Arf-GAP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00288","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 104 |
| Details | Domain: {"description":"PH 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00145","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 23 |
| Details | Zinc finger: {"description":"C4-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00288","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"12893243","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"PubMed","id":"12893243","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
