6YVS

FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH 5-{4-[(Pyridin-3-ylmethyl)-amino]-5-trifluoromethyl-pyrimidin-2-ylamino}-1,3-dihydro-indol-2-one

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
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue PVT A 701

Chain	Residue
A	ARG426
A	LEU553
A	HOH933
A	ILE428
A	VAL436
A	ALA452
A	MET499
A	LEU501
A	CYS502
A	THR503
A	GLY505

---

site_id	AC2
Number of Residues	13
Details	binding site for residue PVT B 701

Chain	Residue
B	ILE428
B	ALA452
B	VAL484
B	MET499
B	GLU500
B	LEU501
B	CYS502
B	THR503
B	GLY505
B	GLU506
B	LEU553
B	HOH917
D	GLN624

---

site_id	AC3
Number of Residues	10
Details	binding site for residue SO4 B 702

Chain	Residue
B	SER601
B	ARG668
B	HOH803
B	HOH815
B	HOH818
B	HOH854
B	HOH884
B	HOH887
D	SER601
D	ARG668

---

site_id	AC4
Number of Residues	11
Details	binding site for residue PVT C 701

Chain	Residue
C	ARG426
C	ILE428
C	ALA452
C	VAL484
C	MET499
C	GLU500
C	LEU501
C	CYS502
C	GLY505
C	ARG550
C	LEU553

---

site_id	AC5
Number of Residues	13
Details	binding site for residue PVT D 701

Chain	Residue
B	ARG514
B	TYR516
B	SER517
D	ARG426
D	ILE428
D	ALA452
D	MET499
D	GLU500
D	CYS502
D	THR503
D	GLY505
D	LEU553
D	ASP564

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP546
B	ASP546
C	ASP546
D	ASP546

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12467573

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

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	TYR570
B	TYR570
C	TYR570
D	TYR570

---

site_id	SWS_FT_FI4
Number of Residues	4
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
C	TYR576
D	TYR576

---

site_id	SWS_FT_FI5
Number of Residues	4
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
C	TYR577
D	TYR577

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER580
B	SER580
C	SER580
D	SER580

---