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Crystal structure of wild type braf kinase domain in complex with organometallic inhibitor CNS292

Analyse Crystal structure of wild type braf kinase domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3Q4C
Type
protein
Length
528 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SERINE/THREONINE-protein kinase B-RAF
EC
2.7.11.1
UniProt
P15056
Ligands
RSW
Pockets
7 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1)protein26439% helix, 14% strandP15056

Ligands and binding sites

  • RSW · [(1,2,3,4,5,6-eta)-(1S,2R,3R,4R,5S,6S)-1-carboxycyclohexane-1,2,3,4,5,6-hexayl](chloro)(3-methyl-5,7-dioxo-6,7-dihydro-5H-pyrido[2,3-a]pyrrolo[3,4-c]carbazol-12-ide-kappa~2~N~1~,N~12~)ruthenium(1+) · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12870.680.8327empty
22870.650.8128RSW
3680.650.9321empty
41470.560.8221empty
5730.510.8516empty

Interfaces

1 interface between chains.

  • A–B · 1168 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 3Q4C · Crystal Structure of Wild Type BRAF kinase domain in complex with organometallic… · the same entry in another collection · chain A against A, TM-score 1.00
  • P15056 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase B-RAF (P15056) · a predicted model of the same protein · chain A against A, TM-score 0.95

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