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5KGK

Crystal structure of PIM1 with inhibitor: 3-(4-methoxyphenyl)-1~{H}-pyrazol-5-amine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0043066biological_processnegative regulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 401
ChainResidue
AILE133
AASP170
AASP234
AGLY238

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 402
ChainResidue
ATRP269
ASER276
AASP277
AARG278
AGLU283

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
AARG136
AALA138
ALEU139
AGLN140
ALEU143

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 404
ChainResidue
AARG221
APRO279
ATHR280
APHE281

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 405
ChainResidue
AGLU262
AHIS265
AHIS287
APRO288

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO A 406
ChainResidue
AGLU141
AGLU142

site_idAC7
Number of Residues6
Detailsbinding site for residue 6SD A 407
ChainResidue
ALEU44
AALA65
ALYS67
ALEU120
AILE185
AASP186

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 A 408
ChainResidue
AARG156
AARG258
ASER261
APHE281
AHOH501

site_idAC9
Number of Residues2
Detailsbinding site for residue SO4 A 409
ChainResidue
AASP108
ATRP109

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK
ChainResidueDetails
ALEU44-LYS67

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI
ChainResidueDetails
AVAL163-ILE175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP167

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU44

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
ChainResidueDetails
AASP128
ALYS67
AGLU121

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054
ChainResidueDetails
ASER261
ASER98

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PDB entries from 2024-06-12

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