5EG3

Crystal Structure of the Activated FGF Receptor 2 (FGFR2) Kinase Domain in complex with the cSH2 domain of Phospholipase C gamma (PLCgamma)

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	17
Details	binding site for residue ACP A 801

Chain	Residue
A	LEU487
A	ASN631
A	LEU633
A	ASP644
A	ARG664
A	MG802
A	MG803
A	HOH901
A	HOH911
A	GLY488
A	ALA515
A	LYS517
A	VAL564
A	ALA565
A	ALA567
A	ASN571
A	ARG630

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site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 802

Chain	Residue
A	ARG630
A	ASN631
A	ACP801
A	MG803

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site_id	AC3
Number of Residues	4
Details	binding site for residue MG A 803

Chain	Residue
A	ASN631
A	ASP644
A	ACP801
A	MG802

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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	LEU487-LYS517

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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	CYS622-VAL634

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by SYK => ECO:0000250|UniProtKB:P08487

Chain	Residue	Details
B	TYR771

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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	LEU487
A	LYS517
A	ALA565
A	ASN571

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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	PHE466
A	PRO588

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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	LEU586
A	PHE656
A	PHE657

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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	PTR769

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