5DFP

Crystal structure of PAK1 in complex with an inhibitor compound FRAX1036

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue 59U A 601

Chain	Residue
A	VAL284
A	LEU347
A	ASP354
A	LEU396
A	THR406
A	DMS602
A	HOH725
A	ARG299
A	MET301
A	GLU315
A	ILE316
A	MET319
A	MET344
A	GLU345
A	TYR346

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site_id	AC2
Number of Residues	4
Details	binding site for residue DMS A 602

Chain	Residue
A	ARG299
A	GLU315
A	ASP407
A	59U601

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL385-LEU397

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22153498

Chain	Residue	Details
A	ASP389

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:22153498

Chain	Residue	Details
A	ILE276
A	ARG299
A	GLU345

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089

Chain	Residue	Details
A	TYR285

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis, BRSK2 and PDPK1 => ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:22669945

Chain	Residue	Details
A	TPO423

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