3GQI

Crystal Structure of activated receptor tyrosine kinase in complex with substrates

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	0005007	molecular_function	fibroblast growth factor receptor activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DVT A 1

Chain	Residue
A	ASP503
B	ARG694
B	ARG696
B	ASN697
B	GLU698
A	LYS504
A	PRO505
A	ASN506
A	ARG507
B	HOH34
B	LEU673
B	THR674
B	ARG675

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site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ACP A 775

Chain	Residue
A	LEU484
A	GLY485
A	GLY487
A	ALA488
A	PHE489
A	GLY490
A	VAL492
A	ALA512
A	LYS514
A	GLU562
A	ALA564
A	ASN568
A	ARG627
A	ASN628
A	LEU630
A	ASP641
A	MG776

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 776

Chain	Residue
A	ASN628
A	ASP641
A	ACP775

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	31
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK

Chain	Residue	Details
A	LEU484-LYS514

---

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

Chain	Residue	Details
A	CYS619-VAL631

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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, ECO:0000269|PubMed:19224897

Chain	Residue	Details
A	ASP623

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	LEU484
A	LYS514
A	GLU562
A	ASN568
A	ARG627
A	ASP641

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Mediates interaction with PLCG1 and SHB

Chain	Residue	Details
A	PTR766

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site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701

Chain	Residue	Details
A	TYR463
A	PHE583
A	PHE585

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701

Chain	Residue	Details
A	PTR653
A	PTR654

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701

Chain	Residue	Details
A	TYR730

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19665973

Chain	Residue	Details
A	PTR766

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG627
A	ASP623

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ALA625
A	ASP623

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	THR658
A	ALA625
A	ASP623

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASN628
A	ALA625
A	ASP623

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