Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3EFW

Structure of AuroraA with pyridyl-pyrimidine urea inhibitor

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
B0000212biological_processmeiotic spindle organization
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007052biological_processmitotic spindle organization
B0007098biological_processcentrosome cycle
B0007100biological_processmitotic centrosome separation
B0051321biological_processmeiotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AK8 A 404
ChainResidue
ALYS143
ATYR212
AALA213
ALEU263
AALA273
ASO4405
AHOH416
APHE144
AVAL147
ALYS162
AVAL174
AGLN177
ALEU178
ALEU210
AGLU211

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AASN261
AASP274
APHE275
AAK8404

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AK8 B 404
ChainResidue
BLYS143
BVAL147
BLYS162
BVAL174
BGLN177
BLEU178
BGLU181
BLEU210
BGLU211
BALA213
BASN261
BLEU263
BALA273
BPHE275
BSO4405
BHOH414

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 405
ChainResidue
BASP274
BPHE275
BAK8404

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337
ChainResidueDetails
AASP256
BASP256

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
ChainResidueDetails
ALYS143
BASP274
ALYS162
AGLU211
AGLU260
AASP274
BLYS143
BLYS162
BGLU211
BGLU260

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197
ChainResidueDetails
ATHR287
BTHR287

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_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
ChainResidueDetails
ATHR288
BTHR288

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726
ChainResidueDetails
ASER342
BSER342

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS258
BLYS258

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon