Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4I41

Crystal Structure of human Ser/Thr kinase Pim1 in complex with mitoxantrone

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 Residues15
DetailsBINDING SITE FOR RESIDUE MIX A 500
ChainResidue
ALEU44
ALYS169
AGLU171
AASN172
ALEU174
AILE185
AASP186
APHE49
AALA65
ALEU120
AGLU121
AGLN127
AASP128
AASP131
AASP167

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MIX A 501
ChainResidue
APHE130
AILE133
ATHR134
ALYS169
AASP170
ATHR204
AASP234
AGLY238
AASP239
AILE240
APRO241
AGLU243
AGLU247
AARG256

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
AASP76

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
ChainResidueDetails
AGLU30
AGLN37

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054
ChainResidueDetails
AASP170

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon