3EFW
Structure of AuroraA with pyridyl-pyrimidine urea inhibitor
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 |
| B | 0000212 | biological_process | meiotic spindle organization |
| B | 0000226 | biological_process | microtubule cytoskeleton organization |
| B | 0000278 | biological_process | mitotic cell cycle |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007052 | biological_process | mitotic spindle organization |
| B | 0007098 | biological_process | centrosome cycle |
| B | 0007100 | biological_process | mitotic centrosome separation |
| B | 0051321 | biological_process | meiotic cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AK8 A 404 |
| Chain | Residue |
| A | LYS143 |
| A | TYR212 |
| A | ALA213 |
| A | LEU263 |
| A | ALA273 |
| A | SO4405 |
| A | HOH416 |
| A | PHE144 |
| A | VAL147 |
| A | LYS162 |
| A | VAL174 |
| A | GLN177 |
| A | LEU178 |
| A | LEU210 |
| A | GLU211 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | ASN261 |
| A | ASP274 |
| A | PHE275 |
| A | AK8404 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AK8 B 404 |
| Chain | Residue |
| B | LYS143 |
| B | VAL147 |
| B | LYS162 |
| B | VAL174 |
| B | GLN177 |
| B | LEU178 |
| B | GLU181 |
| B | LEU210 |
| B | GLU211 |
| B | ALA213 |
| B | ASN261 |
| B | LEU263 |
| B | ALA273 |
| B | PHE275 |
| B | SO4405 |
| B | HOH414 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 405 |
| Chain | Residue |
| B | ASP274 |
| B | PHE275 |
| B | AK8404 |
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 | 2 |
| 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 | 12 |
| 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 | 2 |
| 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 | 4 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP256 | |
| A | GLU260 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP256 | |
| B | GLU260 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS258 | |
| A | ASP256 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS258 | |
| B | ASP256 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS258 | |
| A | ASN261 | |
| A | ASP256 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS258 | |
| B | ASN261 | |
| B | ASP256 |
