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4C2W

Crystal structure of Aurora B in complex with AMP-PNP

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 Residues17
DetailsBINDING SITE FOR RESIDUE ANP A 1001
ChainResidue
AGLY100
APHE172
AALA173
AGLU177
ALEU223
AHOH2010
AHOH2117
AHOH2342
AHOH2343
ALYS101
AGLY102
ALYS103
AVAL107
AALA120
ALYS122
ALEU154
AGLU171

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ANP B 1002
ChainResidue
BLEU99
BPHE104
BGLU171
BPHE172
BALA173
BPRO174
BARG175
BGLY176
BGLU177
BHOH2293

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

219515

PDB entries from 2024-05-08

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