5GRN

Crystal structure of PDGFRA in Complex with WQ-C-159

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	19
Details	binding site for residue 748 A 1001

Chain	Residue
A	LEU599
A	CYS814
A	VAL815
A	HIS816
A	LEU825
A	ILE834
A	CYS835
A	ASP836
A	PHE837
A	HOH1131
A	HOH1235
A	ALA625
A	LYS627
A	GLU644
A	MET648
A	ILE672
A	THR674
A	TYR676
A	CYS677

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site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 1002

Chain	Residue
A	PRO918
A	ASP919
A	HOH1394

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site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 1003

Chain	Residue
A	LYS623
A	PHE678

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU599-LYS627

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

Chain	Residue	Details
A	CYS814-LEU826

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

Chain	Residue	Details
A	GLY652-THR665

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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	ASP818

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU599
A	LYS627

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein

Chain	Residue	Details
A	MET578

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10734113

Chain	Residue	Details
A	TYR572
A	TYR574

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11095946, ECO:0000269|PubMed:8943348

Chain	Residue	Details
A	LEU792

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:1646396

Chain	Residue	Details
A	ALA803
A	CYS814

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17604334

Chain	Residue	Details
A	LEU826

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10733900

Chain	Residue	Details
A	ILE834

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site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8617789

Chain	Residue	Details
A	ALA840

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250

Chain	Residue	Details
A	TYR849

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