6YR9

FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH N-Methyl-N-(2-{[2-(2-oxo-2,3-dihydro-1H-indol-5-ylamino)-5-trifluoromethyl-pyrimidin-4-ylamino]-methyl}-phenyl)-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
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	19
Details	binding site for residue P9K A 701

Chain	Residue
A	ILE428
A	GLU506
A	ARG550
A	ASN551
A	LEU553
A	GLY563
A	ASP564
A	LEU567
A	SER568
D	GLN624
D	GLY625
A	GLU430
A	VAL436
A	ALA452
A	MET499
A	GLU500
A	LEU501
A	CYS502
A	GLY505

---

site_id	AC2
Number of Residues	19
Details	binding site for residue P9K B 701

Chain	Residue
B	ARG426
B	ILE428
B	GLU430
B	VAL436
B	GLN438
B	ALA452
B	MET499
B	GLU500
B	LEU501
B	CYS502
B	GLY505
B	GLU506
B	ARG550
B	ASN551
B	LEU553
B	GLY563
B	ASP564
B	LEU567
B	SER568

---

site_id	AC3
Number of Residues	19
Details	binding site for residue P9K C 701

Chain	Residue
C	ARG426
C	ILE428
C	GLU430
C	VAL436
C	GLN438
C	ALA452
C	MET499
C	GLU500
C	LEU501
C	CYS502
C	GLY505
C	GLU506
C	ARG550
C	ASN551
C	LEU553
C	GLY563
C	ASP564
C	LEU567
C	SER568

---

site_id	AC4
Number of Residues	16
Details	binding site for residue P9K D 701

Chain	Residue
A	TYR516
D	ARG426
D	GLU430
D	ALA452
D	MET499
D	GLU500
D	LEU501
D	CYS502
D	GLY505
D	ARG550
D	ASN551
D	LEU553
D	GLY563
D	ASP564
D	LEU567
D	HOH835

---

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

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