6KLA

Crystal structure of human c-KIT kinase domain in complex with compound 15a

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	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue DJX A 1001

Chain	Residue
A	LEU595
A	LEU799
A	ASP810
A	ALA621
A	LYS623
A	THR670
A	GLU671
A	TYR672
A	CYS673
A	GLY676
A	ASP760

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtaygliksdaamt.....VAVK

Chain	Residue	Details
A	LEU595-LYS623

---

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

Chain	Residue	Details
A	CYS788-LEU800

---

site_id	PS00240
Number of Residues	14
Details	RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GnHmNIVNLLGACT

Chain	Residue	Details
A	GLY648-THR661

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP792

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING:

Chain	Residue	Details
A	GLY596
A	LYS623
A	GLU671
A	ARG796
A	ASN797
A	ASP810
A	TYR568

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:20147452

Chain	Residue	Details
A	TYR547
A	TYR553

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210

Chain	Residue	Details
A	TYR568

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210

Chain	Residue	Details
A	TYR570

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802

Chain	Residue	Details
A	SER821

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452

Chain	Residue	Details
A	TYR823

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163

Chain	Residue	Details
A	SER891

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452

Chain	Residue	Details
A	TYR900

---