6Z4Y
Crystal structure of Aurora A (STK6) in complex with macrocycle ODS2003208
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000212 | biological_process | meiotic spindle organization |
| A | 0000226 | biological_process | microtubule cytoskeleton organization |
| A | 0000278 | biological_process | mitotic cell cycle |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007052 | biological_process | mitotic spindle organization |
| A | 0007098 | biological_process | centrosome cycle |
| A | 0007100 | biological_process | mitotic centrosome separation |
| A | 0051321 | biological_process | meiotic cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue CIT A 501 |
| Chain | Residue |
| A | SER266 |
| A | THR333 |
| A | GLU336 |
| A | GLU336 |
| A | LYS339 |
| A | ARG340 |
| A | ARG343 |
| A | HOH639 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue CIT A 502 |
| Chain | Residue |
| A | GLU175 |
| A | HIS176 |
| A | ARG180 |
| A | ARG180 |
| A | HIS280 |
| A | ALA281 |
| A | HOH603 |
| A | GLY173 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | GLN177 |
| A | GLU181 |
| A | HOH624 |
| A | HOH641 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | HOH619 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | HIS248 |
| A | LYS309 |
| A | LEU374 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | PRO191 |
| A | GLU269 |
| A | LYS271 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | LEU139 |
| A | GLY216 |
| A | THR217 |
| A | HOH672 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue Q7Q A 508 |
| Chain | Residue |
| A | LYS141 |
| A | GLY142 |
| A | ALA160 |
| A | LYS162 |
| A | LEU208 |
| A | LEU210 |
| A | GLU211 |
| A | TYR212 |
| A | ALA213 |
| A | THR217 |
| A | ASN261 |
| A | LEU263 |
| A | ALA273 |
| A | PHE275 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK |
| Chain | Residue | Details |
| A | LEU139-LYS162 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL |
| Chain | Residue | Details |
| A | VAL252-LEU264 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27837025","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G1X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
