3CLY

Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction

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	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1801

Chain	Residue
A	ASN1631
A	ASP1644
A	ACP1803
A	HOH1901
A	HOH1902

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 1802

Chain	Residue
A	GLU1534
A	ASP1644
A	GLY1646
A	ACP1803

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site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ACP A 1803

Chain	Residue
A	LEU1487
A	GLY1488
A	GLN1494
A	VAL1495
A	ALA1515
A	LYS1517
A	VAL1564
A	GLU1565
A	ALA1567
A	ASN1571
A	ARG1630
A	ASN1631
A	LEU1633
A	ASP1644
A	MG1801
A	MG1802
A	HOH1901
A	HOH1912
A	HOH1916
A	HOH1922
A	HOH1939
A	HOH1978
A	HOH1985
A	HOH1986

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU1487-LYS1517

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

Chain	Residue	Details
A	CYS1622-VAL1634

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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:19060208

Chain	Residue	Details
A	ASP1626

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208

Chain	Residue	Details
A	LEU1487
A	LYS1517
A	GLU1565
A	ASN1571

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646

Chain	Residue	Details
A	TYR1466
A	TYR1588

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646

Chain	Residue	Details
A	TYR1586
A	PTR1656
A	PTR1657

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:19060208

Chain	Residue	Details
A	TYR1769

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG1630
A	ASP1626

---

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

Chain	Residue	Details
A	ALA1628
A	ASP1626

---

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

Chain	Residue	Details
A	ALA1628
A	THR1661
A	ASP1626

---

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

Chain	Residue	Details
A	ASN1631
A	ALA1628
A	ASP1626

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