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4C2V

Aurora B kinase in complex with the specific inhibitor Barasertib

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 Residues18
DetailsBINDING SITE FOR RESIDUE YJA A 1357
ChainResidue
APHE104
APHE172
AALA173
APRO174
AGLY176
ALEU223
AALA233
AHOH2012
AHOH2043
AHOH2096
ALYS122
ALEU138
AGLU141
AGLN145
ALEU154
AMET156
ALEU168
AGLU171

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE YJA B 1357
ChainResidue
BLEU99
BPHE104
BLYS122
BLEU138
BGLU141
BGLN145
BLEU154
BMET156
BLEU168
BLEU170
BGLU171
BPHE172
BALA173
BPRO174
BGLY176
BLEU223
BALA233
BHOH2108
BHOH2110

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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