4XV3

B-Raf Kinase V600E oncogenic mutant in complex with PLX7922

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue P02 A 801

Chain	Residue
A	VAL471
A	CYS532
A	ASP594
A	PHE595
A	GLY596
A	ALA481
A	LYS483
A	LEU505
A	LEU514
A	ILE527
A	THR529
A	GLN530
A	TRP531

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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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP576
B	ASP576

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE463
A	LYS483
B	ILE463
B	LYS483

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	ALA446
B	ALA446

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	ALA447
B	ALA447

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714

Chain	Residue	Details
A	ARG671
B	ARG671

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site_id	SWS_FT_FI6
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581

Chain	Residue	Details
A	LYS578
B	LYS578

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