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5KGD

Crystal structure of PIM1 with inhibitor: 2-pyridin-3-yl-1~{H}-benzimidazole

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 Residues6
Detailsbinding site for residue EDO A 402
ChainResidue
A6SL420
AGLU89
ALEU93
AILE185
AASP186
APHE187

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 403
ChainResidue
AARG136
AALA138
ALEU139
AGLN140
ALEU143
AHOH521

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 404
ChainResidue
AARG221
ASER222
AVAL225
AARG278
APRO279
AHOH514
AHOH559

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 405
ChainResidue
APHE100
AGLU153
AASN160
AGLN264
AARG268

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO A 406
ChainResidue
AGLU35
AVAL40
AHIS68
AHOH535

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 407
ChainResidue
AASP114
ALEU193
AEDO419
AHOH563

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO A 408
ChainResidue
AASP170
AGLU171
ATYR207
AILE240

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 409
ChainResidue
AGLU181
AGLN252
AVAL253
APHE254

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 410
ChainResidue
ALYS169
AGLU171
ATHR204
AHOH532

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO A 411
ChainResidue
AGLY99
AARG250
AGLY251
AGLN252

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO A 412
ChainResidue
AGLU262
AHIS265
AHIS287
APRO288
AEDO416

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO A 413
ChainResidue
AGLU142
AARG145
AHOH520

site_idAD5
Number of Residues6
Detailsbinding site for residue EDO A 414
ChainResidue
ALEU43
AHIS219
AARG221
ASER222
APRO275
AEDO418

site_idAD6
Number of Residues1
Detailsbinding site for residue EDO A 415
ChainResidue
ALEU177

site_idAD7
Number of Residues7
Detailsbinding site for residue EDO A 416
ChainResidue
ATRP269
AGLU283
AASN286
AHIS287
APRO288
AEDO412
AHOH543

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO A 417
ChainResidue
AHIS265
ATRP269
AHOH561

site_idAD9
Number of Residues7
Detailsbinding site for residue EDO A 418
ChainResidue
ATYR53
ALEU193
ALYS194
AGLY220
AARG221
AEDO414
AHOH542

site_idAE1
Number of Residues2
Detailsbinding site for residue EDO A 419
ChainResidue
AEDO407
AHOH529

site_idAE2
Number of Residues9
Detailsbinding site for residue 6SL A 420
ChainResidue
APHE49
AALA65
ALYS67
AGLU121
ALEU174
AILE185
AASP186
AEDO402
AHOH570

site_idAE3
Number of Residues7
Detailsbinding site for residue SO4 A 421
ChainResidue
AHOH501
AHOH537
AHOH557
AARG156
AARG258
ASER261
APHE281

site_idAE4
Number of Residues3
Detailsbinding site for residue SO4 A 422
ChainResidue
AASP108
ATRP109
AHOH524

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
ALYS67
AGLU121
AASP128

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

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PDB entries from 2024-10-09

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