6YT6

FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH N-Methyl-N-(3-{[2-(2-oxo-2,3-dihydro-1H-indol-5-ylamino)-pyrimidin-4-ylamino]-methyl}-pyridin-2-yl)-methanesulfonamide

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	15
Details	binding site for residue PKE A 701

Chain	Residue
A	ARG426
A	GLY505
A	GLU506
A	ARG550
A	LEU553
A	GLY563
A	HOH819
A	ILE428
A	GLY429
A	GLU430
A	VAL436
A	GLN438
A	GLU500
A	LEU501
A	CYS502

---

site_id	AC2
Number of Residues	9
Details	binding site for residue SO4 A 702

Chain	Residue
A	SER601
A	ARG668
A	HOH801
A	HOH802
A	HOH804
A	HOH821
A	HOH881
B	SER601
B	ARG668

---

site_id	AC3
Number of Residues	15
Details	binding site for residue PKE B 701

Chain	Residue
B	ARG426
B	GLY429
B	GLU430
B	VAL436
B	ALA452
B	GLU500
B	LEU501
B	CYS502
B	GLY505
B	GLU506
B	ARG550
B	LEU553
B	GLY563
B	HOH810
B	HOH823

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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

---

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

---

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

---

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	GLU500
B	ILE428
B	LYS454
B	GLU500
A	LYS454
A	ILE428

---

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

Chain	Residue	Details
B	TYR570
A	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
B	TYR576
A	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
B	SER580
A	SER580

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