6GCX

Focal Adhesion Kinase catalytic domain in complex with irreversible inhibitor

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue EUW A 701

Chain	Residue
A	ARG426
A	ASP564
A	LEU567
A	HOH809
A	GLN438
A	GLU500
A	LEU501
A	CYS502
A	LEU504
A	GLY505
A	LEU553
A	GLY563

---

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 702

Chain	Residue
A	ILE635
A	GLU636
A	TYR661
A	HOH802
A	HOH861

---

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 703

Chain	Residue
A	THR670
A	GLU671
A	ALA674
A	HOH806

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	HIS544-SER574

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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