3W2C
Structure of Aurora kinase A complexed to benzoimidazole-indazole inhibitor XV
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 |
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 |
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 |
G | 0000212 | biological_process | meiotic spindle organization |
G | 0000226 | biological_process | microtubule cytoskeleton organization |
G | 0000278 | biological_process | mitotic cell cycle |
G | 0004672 | molecular_function | protein kinase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006468 | biological_process | protein phosphorylation |
G | 0007052 | biological_process | mitotic spindle organization |
G | 0007098 | biological_process | centrosome cycle |
G | 0007100 | biological_process | mitotic centrosome separation |
G | 0051321 | biological_process | meiotic cell cycle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE N15 A 401 |
Chain | Residue |
A | ARG137 |
A | TYR212 |
A | ALA213 |
A | GLY216 |
A | LEU263 |
A | ALA273 |
A | ASP274 |
A | HOH509 |
A | LEU139 |
A | PHE144 |
A | VAL147 |
A | LYS162 |
A | GLN185 |
A | LEU194 |
A | LEU210 |
A | GLU211 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE N15 C 401 |
Chain | Residue |
C | LEU139 |
C | LYS162 |
C | VAL182 |
C | GLN185 |
C | LEU194 |
C | LEU210 |
C | GLU211 |
C | TYR212 |
C | ALA213 |
C | GLY216 |
C | LEU263 |
C | ALA273 |
C | ASP274 |
C | HOH532 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE N15 E 401 |
Chain | Residue |
E | LEU139 |
E | LYS162 |
E | GLN185 |
E | LEU194 |
E | LEU208 |
E | GLU211 |
E | TYR212 |
E | ALA213 |
E | GLY216 |
E | LEU263 |
E | ASP274 |
E | HOH515 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE N15 G 401 |
Chain | Residue |
G | LEU139 |
G | PHE144 |
G | LYS162 |
G | GLN185 |
G | LEU194 |
G | LEU210 |
G | GLU211 |
G | TYR212 |
G | ALA213 |
G | GLY216 |
G | LEU263 |
G | ASP274 |
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 | 24 |
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_FI2 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
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 |