Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3W2C

Structure of Aurora kinase A complexed to benzoimidazole-indazole inhibitor XV

Functional Information from GO Data
ChainGOidnamespacecontents
A0000212biological_processmeiotic spindle organization
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007052biological_processmitotic spindle organization
A0007098biological_processcentrosome cycle
A0007100biological_processmitotic centrosome separation
A0051321biological_processmeiotic cell cycle
C0000212biological_processmeiotic spindle organization
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0007052biological_processmitotic spindle organization
C0007098biological_processcentrosome cycle
C0007100biological_processmitotic centrosome separation
C0051321biological_processmeiotic cell cycle
E0000212biological_processmeiotic spindle organization
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
E0007052biological_processmitotic spindle organization
E0007098biological_processcentrosome cycle
E0007100biological_processmitotic centrosome separation
E0051321biological_processmeiotic cell cycle
G0000212biological_processmeiotic spindle organization
G0000226biological_processmicrotubule cytoskeleton organization
G0000278biological_processmitotic cell cycle
G0004672molecular_functionprotein kinase activity
G0005524molecular_functionATP binding
G0006468biological_processprotein phosphorylation
G0007052biological_processmitotic spindle organization
G0007098biological_processcentrosome cycle
G0007100biological_processmitotic centrosome separation
G0051321biological_processmeiotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE N15 A 401
ChainResidue
AARG137
ATYR212
AALA213
AGLY216
ALEU263
AALA273
AASP274
AHOH509
ALEU139
APHE144
AVAL147
ALYS162
AGLN185
ALEU194
ALEU210
AGLU211

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE N15 C 401
ChainResidue
CLEU139
CLYS162
CVAL182
CGLN185
CLEU194
CLEU210
CGLU211
CTYR212
CALA213
CGLY216
CLEU263
CALA273
CASP274
CHOH532

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE N15 E 401
ChainResidue
ELEU139
ELYS162
EGLN185
ELEU194
ELEU208
EGLU211
ETYR212
EALA213
EGLY216
ELEU263
EASP274
EHOH515

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE N15 G 401
ChainResidue
GLEU139
GPHE144
GLYS162
GGLN185
GLEU194
GLEU210
GGLU211
GTYR212
GALA213
GGLY216
GLEU263
GASP274

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK
ChainResidueDetails
ALEU139-LYS162

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL
ChainResidueDetails
AVAL252-LEU264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27837025","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G1X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon