1UWH: The complex of wild type B-RAF and BAY439006

The complex of wild type B-RAF and BAY439006. Determined by X-ray diffraction at 2.95 Å resolution. Released 19 Mar 2004.

Method: X-ray diffraction
Resolution: 2.95 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 4,290
Mol. weight: 63.81 kDa
Ligands: BAX
Released: 19 Mar 2004

Explore 1UWH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1UWH contains 32 α-helices and 20 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	450	1	1
α-helix	451-452	2
β-strand	461-464	4	1
β-strand	469-474	6	1
β-strand	478-483	6	1
α-helix	493-504	12
β-strand	512	1	2
β-strand	515-519	5	1
β-strand	525-529	5	1
α-helix	530-532	3
β-strand	533-535	3	2
α-helix	536-537	2
α-helix	538-542	5
α-helix	549-568	20
α-helix	578-580	3
β-strand	581-584	4	2
β-strand	589-591	3	2
α-helix	616-618	3
α-helix	621-624	4
α-helix	634-650	17
α-helix	661-670	10
α-helix	677-679	3
α-helix	686-695	10
α-helix	700-702	3
α-helix	704-705	2
α-helix	706-718	13

Chain B: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	450	1	3
α-helix	451-452	2
β-strand	461-465	5	3
β-strand	468-474	7	3
β-strand	478-483	6	3
α-helix	493-504	12
β-strand	512	1	4
β-strand	515-519	5	3
β-strand	525-529	5	3
α-helix	530-532	3
β-strand	533-535	3	4
α-helix	536-537	2
α-helix	538-542	5
α-helix	549-568	20
α-helix	578-580	3
β-strand	581-584	4	4
β-strand	589-591	3	4
α-helix	616-618	3
α-helix	621-624	4
α-helix	634-650	17
α-helix	661-670	10
α-helix	677-679	3
α-helix	686-695	10
α-helix	700-702	3
α-helix	704-705	2
α-helix	706-718	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
B-raf proto-oncogene serine/threonine-protein kinase	A, B	protein	276	HOMO SAPIENS	P15056 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1UWH_1 B-RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE (chains A, B)
DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRK
TRHVNILLFMGYSTAPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYL
HAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRM
QDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPK
AMKRLMAECLKKKRDERPLFPQILASIELLARSLPK

Ligands and cofactors

ID	Name	Formula	Copies
BAX	4-{4-[({[4-chloro-3-(trifluoromethyl)phenyl]amino}carbonyl)amino]phenoxy}-N-met…	C21 H16 Cl F3 N4 O3	2

Water and common crystallization additives (CL) are not listed.

Primary citation

Mechanism of Activation of the Raf-Erk Signaling Pathway by Oncogenic Mutations of B-Raf. Wan, P.T.C., Garnett, M.J., Roe, S.M. et al. Cell (2004) 116:855. DOI 10.1016/S0092-8674(04)00215-6 · PubMed

Other PDB entries of the same protein (UniProt P15056 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8VSO 1.5 Å, Ternary structure of 14-3-3 sigma, BRAF phosphopeptide (pS365) and compound 78 (1124378)
8JNB 1.62 Å, CRAF ras-binding domain chimera, ligand complex
8C7X 1.65 Å, Crystal structure of BRAF in complex with a hybrid compound 6
8C7Y 1.65 Å, Crystal structure of BRAF V600E in complex with a hybrid compound 6
9EW6 1.65 Å, Binary structure of 14-3-3s and BRAF phosphopeptide (pS365)
8JNA 1.7 Å, CRAF ras-binding domain chimera, apo form
9BP8 1.73 Å, Crystal structure of BRAF kinase domain with PF-07799933
5VYK 1.75 Å, Crystal structure of the BRS domain of BRAF in complex with the CC-SAM domain of KSR1
9BFB 1.92 Å, Crystal structure of BRAF kinase domain with PF-07284890
7K0V 1.93 Å, Crystal structure of bRaf in complex with inhibitor GNE-0749
5ITA 1.95 Å, Crystal Structure of BRAF Kinase Domain Bound to AZ-VEM
3NY5 1.99 Å, Crystal structure of the RBD domain of serine/threonine-protein kinase B-raf from Homo…

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1UWH is part of these collections:

Kinases and cancer drug targets

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