2BMC
Aurora-2 T287D T288D complexed with PHA-680632
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 |
| C | 0000212 | biological_process | meiotic spindle organization |
| C | 0000226 | biological_process | microtubule cytoskeleton organization |
| C | 0000278 | biological_process | mitotic cell cycle |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0007052 | biological_process | mitotic spindle organization |
| C | 0007098 | biological_process | centrosome cycle |
| C | 0007100 | biological_process | mitotic centrosome separation |
| C | 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 |
| E | 0000212 | biological_process | meiotic spindle organization |
| E | 0000226 | biological_process | microtubule cytoskeleton organization |
| E | 0000278 | biological_process | mitotic cell cycle |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| E | 0007052 | biological_process | mitotic spindle organization |
| E | 0007098 | biological_process | centrosome cycle |
| E | 0007100 | biological_process | mitotic centrosome separation |
| E | 0051321 | biological_process | meiotic cell cycle |
| F | 0000212 | biological_process | meiotic spindle organization |
| F | 0000226 | biological_process | microtubule cytoskeleton organization |
| F | 0000278 | biological_process | mitotic cell cycle |
| F | 0004672 | molecular_function | protein kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006468 | biological_process | protein phosphorylation |
| F | 0007052 | biological_process | mitotic spindle organization |
| F | 0007098 | biological_process | centrosome cycle |
| F | 0007100 | biological_process | mitotic centrosome separation |
| F | 0051321 | biological_process | meiotic cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MPY A1395 |
| Chain | Residue |
| A | GLY140 |
| A | PRO214 |
| A | GLY216 |
| A | GLU260 |
| A | ASN261 |
| A | LEU263 |
| B | SER266 |
| B | ALA267 |
| B | GLY268 |
| A | LYS141 |
| A | GLY142 |
| A | VAL147 |
| A | ALA160 |
| A | LYS162 |
| A | GLU211 |
| A | TYR212 |
| A | ALA213 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MPY B1395 |
| Chain | Residue |
| B | GLY140 |
| B | LYS141 |
| B | VAL147 |
| B | ALA160 |
| B | LYS162 |
| B | GLU211 |
| B | TYR212 |
| B | ALA213 |
| B | PRO214 |
| B | GLY216 |
| B | LYS224 |
| B | GLU260 |
| B | ASN261 |
| B | LEU263 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE MPY C1394 |
| Chain | Residue |
| C | GLY140 |
| C | LYS141 |
| C | GLY142 |
| C | VAL147 |
| C | ALA160 |
| C | LYS162 |
| C | LEU194 |
| C | GLU211 |
| C | TYR212 |
| C | ALA213 |
| C | PRO214 |
| C | GLY216 |
| C | GLU260 |
| C | ASN261 |
| C | LEU263 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE MPY D1395 |
| Chain | Residue |
| C | LEU215 |
| D | GLY140 |
| D | LYS141 |
| D | VAL147 |
| D | ALA160 |
| D | LYS162 |
| D | GLU211 |
| D | TYR212 |
| D | ALA213 |
| D | PRO214 |
| D | GLY216 |
| D | THR217 |
| D | GLU260 |
| D | ASN261 |
| D | LEU263 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MPY E1395 |
| Chain | Residue |
| E | GLY140 |
| E | LYS141 |
| E | GLY142 |
| E | VAL147 |
| E | ALA160 |
| E | LYS162 |
| E | GLU211 |
| E | TYR212 |
| E | ALA213 |
| E | PRO214 |
| E | GLY216 |
| E | GLU260 |
| E | ASN261 |
| E | LEU263 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MPY F1395 |
| Chain | Residue |
| E | SER266 |
| F | LEU139 |
| F | GLY140 |
| F | VAL147 |
| F | ALA160 |
| F | LYS162 |
| F | GLU211 |
| F | TYR212 |
| F | ALA213 |
| F | PRO214 |
| F | GLU260 |
| F | ASN261 |
| F | LEU263 |
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 | 6 |
| 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 | 36 |
| 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 | 6 |
| 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 | 12 |
| 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 | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS258 | |
| D | ASP256 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | LYS258 | |
| E | ASP256 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | LYS258 | |
| F | ASP256 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR292 | |
| A | LYS258 | |
| A | ASP256 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR292 | |
| B | LYS258 | |
| B | ASP256 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | THR292 | |
| C | LYS258 | |
| C | ASP256 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | THR292 | |
| D | LYS258 | |
| D | ASP256 |
| site_id | CSA17 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | THR292 | |
| E | LYS258 | |
| E | ASP256 |
| site_id | CSA18 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | THR292 | |
| F | LYS258 | |
| F | ASP256 |
| site_id | CSA19 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS258 | |
| A | ASN261 | |
| A | 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 | CSA20 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS258 | |
| B | ASN261 | |
| B | ASP256 |
| site_id | CSA21 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | LYS258 | |
| C | ASN261 | |
| C | ASP256 |
| site_id | CSA22 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS258 | |
| D | ASN261 | |
| D | ASP256 |
| site_id | CSA23 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | LYS258 | |
| E | ASN261 | |
| E | ASP256 |
| site_id | CSA24 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | LYS258 | |
| F | ASN261 | |
| F | ASP256 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP256 | |
| C | GLU260 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP256 | |
| D | GLU260 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| E | ASP256 | |
| E | GLU260 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| F | ASP256 | |
| F | GLU260 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS258 | |
| A | ASP256 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS258 | |
| B | ASP256 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | LYS258 | |
| C | ASP256 |
