4LMU

Crystal structure of Pim1 in complex with the inhibitor Quercetin (resulting from displacement of SKF86002)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006338	biological_process	chromatin remodeling
A	0006468	biological_process	protein phosphorylation
A	0006915	biological_process	apoptotic process
A	0008134	molecular_function	transcription factor binding
A	0016310	biological_process	phosphorylation
A	0022898	biological_process	regulation of transmembrane transporter activity
A	0030145	molecular_function	manganese ion binding
A	0043024	molecular_function	ribosomal small subunit binding
A	0043066	biological_process	negative regulation of apoptotic process
A	0043433	biological_process	negative regulation of DNA-binding transcription factor activity
A	0044024	molecular_function	histone H2AS1 kinase activity
A	0045824	biological_process	negative regulation of innate immune response
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0046777	biological_process	protein autophosphorylation
A	0046872	molecular_function	metal ion binding
A	0050821	biological_process	protein stabilization
A	0060045	biological_process	positive regulation of cardiac muscle cell proliferation
A	0070561	biological_process	vitamin D receptor signaling pathway
A	0071346	biological_process	cellular response to type II interferon
A	0090336	biological_process	positive regulation of brown fat cell differentiation
A	0106310	molecular_function	protein serine kinase activity
A	1902033	biological_process	regulation of hematopoietic stem cell proliferation
A	1904263	biological_process	positive regulation of TORC1 signaling
A	1905062	biological_process	positive regulation of cardioblast proliferation
A	1990748	biological_process	cellular detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE QUE A 401

Chain	Residue
A	LEU44
A	VAL126
A	LEU174
A	ILE185
A	ASP186
A	HOH538
A	ALA65
A	LYS67
A	GLU89
A	ILE104
A	LEU120
A	GLU121
A	ARG122
A	PRO123

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 402

Chain	Residue
A	PHE130
A	THR134
A	ASP170
A	ASP234
A	GLY238
A	ASP239

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK

Chain	Residue	Details
A	LEU44-LYS67

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI

Chain	Residue	Details
A	VAL163-ILE175

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP76

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862

Chain	Residue	Details
A	GLU30
A	GLN37

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054

Chain	Residue	Details
A	ASP170

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