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Crystal structure of PAK1 kinase domain with ruthenium complex DW1

Analyse Crystal structure of PAK1 kinase domain with ruthenium complex DW1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FY0
Type: protein
Length: 293 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase pak 1
EC: 2.7.11.1
UniProt: Q13153
Ligands: DW1
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase pak 1 (EC 2.7.11.1)	protein	293	44% helix, 17% strand	Q13153

Ligands and binding sites

DW1 · Ruthenium pyridocarbazole · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	329	0.59	0.77	38	DW1

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

3FY0 · Crystal structure of PAK1 kinase domain with ruthenium complex DW1 · the same entry in another collection · chain A against A, TM-score 1.00
Q13153 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase pak 1 (Q13153) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q13153
Elsewhere: RCSB PDB 3FY0 · PDBe 3FY0 · UniProt Q13153

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