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Structure of pectenotoxin-2 bound to actin

Analyse Structure of pectenotoxin-2 bound to actin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Q0R
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Actin
UniProt: P68135
Ligands: ATP, PXT, CA
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Actin	protein	360	44% helix, 21% strand	P68135

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
PXT · Pectenotoxin-2 · ligand · chains A
CA · Calcium ion · metal · 4 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	386	0.72	0.83	52	CA, ATP
2	100	0.50	0.81	22	empty
3	62	0.28	0.74	13	empty

Compared structures

2Q0R · Structure of Pectenotoxin-2 Bound to Actin · the same entry in another collection · chain A against A, TM-score 1.00
P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P68135
Elsewhere: RCSB PDB 2Q0R · PDBe 2Q0R · UniProt P68135

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