3H10
Aurora A inhibitor complex
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 |
| D | 0000212 | biological_process | meiotic spindle organization |
| D | 0000226 | biological_process | microtubule cytoskeleton organization |
| D | 0000278 | biological_process | mitotic cell cycle |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0007052 | biological_process | mitotic spindle organization |
| D | 0007098 | biological_process | centrosome cycle |
| D | 0007100 | biological_process | mitotic centrosome separation |
| D | 0051321 | biological_process | meiotic cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 97B A 1 |
| Chain | Residue |
| A | HOH15 |
| A | ARG220 |
| A | GLU260 |
| A | ASN261 |
| A | LEU263 |
| A | ASP274 |
| A | PHE275 |
| A | VAL279 |
| A | ARG137 |
| A | LYS141 |
| A | VAL147 |
| A | GLU211 |
| A | TYR212 |
| A | ALA213 |
| A | PRO214 |
| A | GLY216 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 97B B 2 |
| Chain | Residue |
| B | HOH53 |
| B | ARG137 |
| B | LEU139 |
| B | LYS141 |
| B | VAL147 |
| B | LYS162 |
| B | GLU211 |
| B | TYR212 |
| B | ALA213 |
| B | PRO214 |
| B | THR217 |
| B | GLU260 |
| B | LEU263 |
| B | ASP274 |
| B | PHE275 |
| B | VAL279 |
| B | HIS366 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 97B D 3 |
| Chain | Residue |
| D | HOH25 |
| D | HOH38 |
| D | ARG137 |
| D | LEU139 |
| D | LYS141 |
| D | VAL147 |
| D | LYS162 |
| D | GLU211 |
| D | TYR212 |
| D | ALA213 |
| D | GLY216 |
| D | ARG220 |
| D | GLU260 |
| D | ASN261 |
| D | LEU263 |
| D | ALA273 |
| D | ASP274 |
| D | PHE275 |
| D | VAL279 |
| D | ARG343 |
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 | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337 |
| Chain | Residue | Details |
| A | ASP256 | |
| B | ASP256 | |
| D | ASP256 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X |
| Chain | Residue | Details |
| A | LYS143 | |
| B | ASP274 | |
| D | LYS143 | |
| D | LYS162 | |
| D | GLU211 | |
| D | GLU260 | |
| D | ASP274 | |
| A | LYS162 | |
| A | GLU211 | |
| A | GLU260 | |
| A | ASP274 | |
| B | LYS143 | |
| B | LYS162 | |
| B | GLU211 | |
| B | GLU260 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197 |
| Chain | Residue | Details |
| A | ALA287 | |
| B | ALA287 | |
| D | ALA287 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606 |
| Chain | Residue | Details |
| A | ALA288 | |
| B | ALA288 | |
| D | ALA288 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726 |
| Chain | Residue | Details |
| A | SER342 | |
| B | SER342 | |
| D | SER342 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS258 | |
| B | LYS258 | |
| D | LYS258 |
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 | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS258 | |
| A | ASN261 | |
| A | ASP256 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS258 | |
| B | ASN261 | |
| B | ASP256 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS258 | |
| D | ASN261 | |
| D | ASP256 |
| 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 |
| D | ASP256 | |
| D | GLU260 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS258 | |
| A | ASP256 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS258 | |
| B | ASP256 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS258 | |
| D | ASP256 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR292 | |
| A | LYS258 | |
| A | ASP256 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR292 | |
| B | LYS258 | |
| B | ASP256 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | THR292 | |
| D | LYS258 | |
| D | ASP256 |
