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5I3R

Crystal Structure of BMP-2-inducible kinase in complex with an Indazole inhibitor

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 Residues16
Detailsbinding site for residue IDK A 401
ChainResidue
AGLY60
AGLY136
AGLN137
AGLU184
AASN185
ACYS197
AASP198
AHOH519
ASER63
AVAL65
AALA77
AMET130
AGLU131
ATYR132
ACYS133
AARG134

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 A 402
ChainResidue
AALA321
AASP322
AHOH526
BHIS49
BGLN50
BTHR70

site_idAC3
Number of Residues18
Detailsbinding site for residue IDK B 401
ChainResidue
BLEU57
BALA58
BGLU59
BSER63
BVAL65
BALA77
BMET130
BGLU131
BTYR132
BCYS133
BARG134
BGLY136
BGLN137
BGLU184
BASN185
BLEU187
BCYS197
BASP198

site_idAC4
Number of Residues5
Detailsbinding site for residue PO4 B 402
ChainResidue
AHIS49
AGLN50
ATHR70
BALA321
BASP322

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKveNILL
ChainResidueDetails
AILE176-LEU188

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
AASP180
BASP180

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU57
ALYS79
BLEU57
BLYS79

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PDB entries from 2024-07-10

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