5K5X

Crystal structure of human PDGFRA

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	4
Details	binding site for residue SO4 A 1001

Chain	Residue
A	LYS917
A	ALA921
A	THR922
A	SER923

---

site_id	AC2
Number of Residues	8
Details	binding site for residue SO4 A 1002

Chain	Residue
A	HOH1102
A	HOH1145
A	HOH1149
A	ARG804
A	LYS959
A	TYR962
A	GLU963
A	HIS966

---

site_id	AC3
Number of Residues	10
Details	binding site for residue SO4 A 1003

Chain	Residue
A	HIS654
A	ARG804
A	HIS966
A	LYS971
A	HOH1102
A	HOH1109
A	HOH1130
A	HOH1157
A	HOH1158
A	HOH1159

---

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

---

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

---

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

---

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

---

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

Chain	Residue	Details
A	LYS627
A	LEU599

---

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	TYR574
A	TYR572

---

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	CYS814
A	ALA803

---

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

Chain	Residue	Details
A	LEU826

---

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

Chain	Residue	Details
A	ILE834

---

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

Chain	Residue	Details
A	ALA840

---

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

Chain	Residue	Details
A	TYR849

---