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6MT0

Crystal structure of human Pim-1 kinase in complex with a quinazolinone-pyrrolodihydropyrrolone inhibitor

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 Residues10
Detailsbinding site for residue JYG A 401
ChainResidue
APHE49
AHOH621
AALA65
ALYS67
ALEU120
AGLU121
AVAL126
ALEU174
AILE185
AASP186

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 402
ChainResidue
AASP108
ATRP109
AHOH508
AHOH548

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
APRO123
AGLU124
AASP176
AARG179

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 Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
ChainResidueDetails
AGLN37

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

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PDB entries from 2024-07-24

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