3PXK

FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH Pyrrolo[2,3-d]thiazole

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PXK A 701

Chain	Residue
A	ILE428
A	GLU430
A	ALA452
A	MET499
A	GLU500
A	CYS502
A	LEU553

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 701

Chain	Residue
A	HOH866
A	HOH883
B	SER601
B	ARG668
B	HOH913
B	HOH943
B	HOH974
A	SER601
A	ARG668

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PXK B 702

Chain	Residue
B	ILE428
B	GLY431
B	ALA452
B	MET499
B	GLU500
B	CYS502
B	ARG550
B	LEU553
B	GLY563
B	ASP564
B	HOH918

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	27
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGQFGDVHqGiymspenpala.......VAIK

Chain	Residue	Details
A	ILE428-LYS454

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site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDIAARNVLV

Chain	Residue	Details
A	PHE542-VAL554

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site_id	PS00661
Number of Residues	31
Details	FERM_2 FERM domain signature 2. HrdiaarnvlVSsndCVklgDfgLsrYMeDS

Chain	Residue	Details
A	HIS544-SER574

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP546
B	ASP546

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12467573

Chain	Residue	Details
A	ILE428
A	LYS454
A	GLU500
B	ILE428
B	LYS454
B	GLU500

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	TYR570
B	TYR570

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by RET and SRC => ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698

Chain	Residue	Details
A	TYR576
B	TYR576

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by RET and SRC => ECO:0000269|PubMed:12387730, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698

Chain	Residue	Details
A	TYR577
B	TYR577

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER580
B	SER580

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