4J97

Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659E Mutation Identified in Endometrial Cancer.

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
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACP A 801

Chain	Residue
A	LEU487
A	GLU489
A	ALA515
A	GLU565
A	TYR566
A	ALA567
A	ASN571
A	LEU633

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 802

Chain	Residue
A	ARG649
A	TYR657
A	ARG664
A	HOH928
A	ARG625

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 803

Chain	Residue
A	ARG577
A	ARG580
A	GLY701
A	SER702

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ACP B 801

Chain	Residue
B	LEU487
B	GLY488
B	GLU489
B	VAL495
B	ALA515
B	VAL564
B	GLU565
B	TYR566
B	ALA567
B	GLY570
B	ASN571
B	ARG630
B	ASN631
B	LEU633
B	HOH902

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 802

Chain	Residue
B	ARG625
B	LEU647
B	ARG649
B	TYR657
B	ARG664

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ACP C 801

Chain	Residue
C	LEU487
C	GLY488
C	PHE492
C	ALA515
C	GLU565
C	TYR566
C	ALA567
C	ASN571
C	LEU633
C	ASP644
C	HOH926
C	HOH927

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 802

Chain	Residue
C	ARG625
C	ARG649
C	TYR657
C	ARG664

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ACP D 801

Chain	Residue
D	LEU487
D	GLY488
D	GLN494
D	ALA515
D	GLU565
D	ALA567
D	ASN571
D	LEU633
D	ASP644

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 802

Chain	Residue
D	ARG625
D	ARG649
D	TYR657
D	ARG664

---

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	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208

Chain	Residue	Details
A	ASP626
B	ASP626
C	ASP626
D	ASP626

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208

Chain	Residue	Details
A	LEU487
C	LYS517
C	GLU565
C	ASN571
D	LEU487
D	LYS517
D	GLU565
D	ASN571
A	LYS517
A	GLU565
A	ASN571
B	LEU487
B	LYS517
B	GLU565
B	ASN571
C	LEU487

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646

Chain	Residue	Details
A	TYR466
A	TYR588
B	TYR466
B	TYR588
C	TYR466
C	TYR588
D	TYR466
D	TYR588

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646

Chain	Residue	Details
A	TYR586
D	TYR586
D	TYR656
D	TYR657
A	TYR656
A	TYR657
B	TYR586
B	TYR656
B	TYR657
C	TYR586
C	TYR656
C	TYR657

---