Research workbench

Crystal structure of the human P21-activated kinase 6

Analyse Crystal structure of the human P21-activated kinase 6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C30
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase pak 6
EC: 2.7.1.37
UniProt: Q9NQU5
Ligands: PO4, CL
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase pak 6 (EC 2.7.1.37)	protein	290	41% helix, 18% strand	Q9NQU5

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
CL · Chloride ion · ion · 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	344	0.57	0.75	44	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

2C30 · Crystal Structure Of The Human P21-Activated Kinase 6 · the same entry in another collection · chain A against A, TM-score 1.00
Q9NQU5 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase pak 6 (Q9NQU5) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q9NQU5
Elsewhere: RCSB PDB 2C30 · PDBe 2C30 · UniProt Q9NQU5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.