7K0V

Crystal structure of bRaf in complex with inhibitor GNE-0749

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	15
Details	binding site for residue VQP A 801

Chain	Residue
A	ALA481
A	CYS532
A	GLY593
A	ASP594
A	PHE595
A	LEU597
D	TRP604
A	LYS483
A	GLU501
A	LEU505
A	LEU514
A	ILE527
A	THR529
A	GLN530
A	TRP531

---

site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 802

Chain	Residue
A	ILE617
A	HOH995
C	GLN493

---

site_id	AC3
Number of Residues	15
Details	binding site for residue VQP B 801

Chain	Residue
B	VAL471
B	ALA481
B	LYS483
B	GLU501
B	LEU505
B	LEU514
B	ILE527
B	THR529
B	GLN530
B	TRP531
B	CYS532
B	GLY593
B	ASP594
B	PHE595
B	LEU597

---

site_id	AC4
Number of Residues	4
Details	binding site for residue CL B 802

Chain	Residue
B	SER616
B	ILE617
B	HOH971
D	GLN493

---

site_id	AC5
Number of Residues	15
Details	binding site for residue VQP C 801

Chain	Residue
C	VAL471
C	ALA481
C	LYS483
C	GLU501
C	LEU505
C	LEU514
C	ILE527
C	THR529
C	GLN530
C	TRP531
C	CYS532
C	GLY593
C	ASP594
C	PHE595
C	HOH977

---

site_id	AC6
Number of Residues	15
Details	binding site for residue VQP D 801

Chain	Residue
D	VAL471
D	ALA481
D	LYS483
D	GLU501
D	LEU505
D	LEU514
D	ILE527
D	THR529
D	GLN530
D	TRP531
D	CYS532
D	GLY593
D	ASP594
D	PHE595
D	HOH956

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	21
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK

Chain	Residue	Details
A	ILE463-LYS483

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL

Chain	Residue	Details
A	ILE572-LEU584

---

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:PRU10027

Chain	Residue	Details
A	ASP576
B	ASP576
C	ASP576
D	ASP576

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE463
A	LYS483
B	ILE463
B	LYS483
C	ILE463
C	LYS483
D	ILE463
D	LYS483

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER446
B	SER446
C	SER446
D	SER446

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER447
B	SER447
C	SER447
D	SER447

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714

Chain	Residue	Details
A	ARG671
B	ARG671
C	ARG671
D	ARG671

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581

Chain	Residue	Details
A	LYS578
B	LYS578
C	LYS578
D	LYS578

---