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5K3Y

Crystal structure of AuroraB/INCENP in complex with BI 811283

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue TPO A 248
ChainResidue
AARG215
AARG246
AARG247
AMET249
ACYS250
AHIS266
AHOH592
AHOH596
DLYS817

site_idAC2
Number of Residues15
Detailsbinding site for residue 6Q4 A 401
ChainResidue
ALEU99
AGLY100
AVAL107
AALA120
ALEU154
ALEU170
AGLU171
APHE172
AALA173
AGLY176
AGLU177
ALEU223
AALA233
AHOH537
AHOH569

site_idAC3
Number of Residues10
Detailsbinding site for residue TPO B 248
ChainResidue
BARG140
BARG215
BARG246
BARG247
BMET249
BCYS250
BMET260
BHIS266
BHOH604
BHOH660

site_idAC4
Number of Residues14
Detailsbinding site for residue 6Q4 B 401
ChainResidue
BLYS101
BGLY102
BVAL107
BALA120
BLEU154
BLEU170
BGLU171
BPHE172
BALA173
BGLY176
BGLU220
BLEU223
BHOH519
BHOH622

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqnkfi..........MALK
ChainResidueDetails
ALEU99-LYS122

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLM
ChainResidueDetails
AVAL212-MET224

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
ChainResidueDetails
AASP216
BASP216

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU99
ALYS122
BLEU99
BLYS122

222415

PDB entries from 2024-07-10

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