6MOB

Crystal structure of KIT1 in complex with DP2976 via co-crystallization

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	6
Details	binding site for residue NO3 A 1001

Chain	Residue
A	ARG586
A	PHE591
A	PRO665
A	LEU667
A	HOH1226
A	HOH1274

---

site_id	AC2
Number of Residues	4
Details	binding site for residue NO3 A 1002

Chain	Residue
A	HOH1184
A	ALA597
A	LYS602
A	LYS626

---

site_id	AC3
Number of Residues	8
Details	binding site for residue NO3 A 1003

Chain	Residue
A	GLY598
A	ALA599
A	PHE600
A	GLY601
A	LEU813
A	ARG815
A	HOH1241
A	HOH1250

---

site_id	AC4
Number of Residues	4
Details	binding site for residue NO3 A 1004

Chain	Residue
A	ARG634
A	PRO665
A	THR666
A	HOH1130

---

site_id	AC5
Number of Residues	5
Details	binding site for residue NO3 A 1005

Chain	Residue
A	THR574
A	GLU635
A	MET638
A	SER639
A	LYS642

---

site_id	AC6
Number of Residues	7
Details	binding site for residue NO3 A 1006

Chain	Residue
A	LYS581
A	TRP582
A	GLU583
A	PHE584
A	LEU657
A	GLY658
A	HOH1142

---

site_id	AC7
Number of Residues	7
Details	binding site for residue NO3 A 1007

Chain	Residue
A	LYS834
A	SER868
A	TYR870
A	PRO871
A	GLY872
A	MET873
A	HOH1133

---

site_id	AC8
Number of Residues	7
Details	binding site for residue NO3 A 1008

Chain	Residue
A	TYR675
A	PHE681
A	ARG684
A	LYS685
A	LEU762
A	ARG804
A	HOH1108

---

site_id	AC9
Number of Residues	5
Details	binding site for residue NO3 A 1009

Chain	Residue
A	ARG683
A	ARG686
A	GLY866
A	SER867
A	HOH1139

---

site_id	AD1
Number of Residues	6
Details	binding site for residue NO3 A 1010

Chain	Residue
A	TRP860
A	PRO871
A	MET889
A	LEU890
A	HOH1118
A	HOH1161

---

site_id	AD2
Number of Residues	6
Details	binding site for residue NO3 A 1011

Chain	Residue
A	TYR870
A	MET873
A	MET882
A	ILE883
A	PHE887
A	ARG888

---

site_id	AD3
Number of Residues	9
Details	binding site for residue NO3 A 1012

Chain	Residue
A	ASN587
A	ARG588
A	TYR609
A	PHE887
A	ARG888
A	HOH1157
A	HOH1159
A	HOH1265
A	HOH1304

---

site_id	AD4
Number of Residues	5
Details	binding site for residue NO3 A 1013

Chain	Residue
A	LYS613
A	ALA616
A	ALA617
A	MET618
A	HOH1102

---

site_id	AD5
Number of Residues	3
Details	binding site for residue NO3 A 1014

Chain	Residue
A	ALA616
A	ALA617
A	GLU885

---

site_id	AD6
Number of Residues	17
Details	binding site for residue JWY A 1015

Chain	Residue
A	VAL603
A	ALA621
A	LYS623
A	GLU640
A	LEU644
A	ILE653
A	VAL654
A	VAL668
A	THR670
A	GLU671
A	CYS673
A	LEU799
A	ILE808
A	CYS809
A	ASP810
A	PHE811
A	HOH1217

---

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	TYR568
A	GLY596
A	LYS623
A	GLU671
A	ARG796
A	ASN797
A	ASP810

---

site_id	SWS_FT_FI3
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_FI4
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_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802

Chain	Residue	Details
A	SER821

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452

Chain	Residue	Details
A	TYR823

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163

Chain	Residue	Details
A	SER891

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452

Chain	Residue	Details
A	TYR900

---