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

---

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

---

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

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"17803937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"15629145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	88
Details	Domain: {"description":"SH2 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by SYK","evidences":[{"source":"UniProtKB","id":"P08487","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---