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Crystal structure of cofilin mutant (COF1-157P)

Analyse Crystal structure of cofilin mutant (COF1-157P) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KED
Type: protein
Length: 262 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cofilin
UniProt: Q03048
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cofilin	protein	131	36% helix, 31% strand	Q03048

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	191	0.49	0.76	34	empty

Interfaces

1 interface between chains.

A–B · 373 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4KED · Crystal Structure of Cofilin Mutant (cof1-157p) · the same entry in another collection · chain A against A, TM-score 1.00
Q03048 · AlphaFold monomer V2.0 prediction for cofilin (Q03048) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q03048
Elsewhere: RCSB PDB 4KED · PDBe 4KED · UniProt Q03048

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