6AGX

The cocrystal structure of FGFR2 bound with compound 14 harboring 5H-pyrrolo[2,3-b]pyrazine scaffold

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein 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	12
Details	binding site for residue 9WX A 800

Chain	Residue
A	LEU487
A	ALA643
A	ASP644
A	PHE645
A	GLY488
A	LYS517
A	GLU534
A	ILE548
A	ALA567
A	ARG630
A	ASN631
A	LEU633

---

site_id	AC2
Number of Residues	14
Details	binding site for residue 9WX B 800

Chain	Residue
B	LEU487
B	GLY488
B	GLY490
B	GLY493
B	ALA515
B	LYS517
B	GLU534
B	ILE548
B	VAL564
B	ALA567
B	LEU633
B	ALA643
B	ASP644
B	PHE645

---

site_id	AC3
Number of Residues	15
Details	binding site for residue 9WX C 800

Chain	Residue
C	LEU487
C	GLY488
C	ALA515
C	LYS517
C	GLU534
C	ILE548
C	VAL562
C	VAL564
C	TYR566
C	ALA567
C	ARG630
C	LEU633
C	ALA643
C	ASP644
C	PHE645

---

site_id	AC4
Number of Residues	13
Details	binding site for residue 9WX D 800

Chain	Residue
D	LEU487
D	GLY488
D	ALA515
D	LYS517
D	GLU534
D	ILE548
D	VAL564
D	ALA567
D	ARG630
D	LEU633
D	ALA643
D	ASP644
D	PHE645

---

Functional Information from PROSITE/UniProt

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

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
B	LEU487
B	LYS517
B	GLU565
B	ASN571
C	LEU487
C	LYS517
C	GLU565
C	ASN571
D	LEU487
D	LYS517
D	GLU565
D	ASN571
A	LEU487
A	LYS517
A	GLU565
A	ASN571

---

site_id	SWS_FT_FI3
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
C	PTR657
D	PTR586
D	PTR656
D	PTR657
A	PTR586
A	PTR656
A	PTR657
B	PTR586
B	PTR656
B	PTR657
C	PTR586
C	PTR656

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646

Chain	Residue	Details
A	PTR588
B	PTR588
C	PTR588
D	PTR588

---