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Fission yeast cofilin

Analyse Fission yeast cofilin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I2Q
Type: protein
Length: 122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cofilin
UniProt: P78929
Ligands: SO4

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cofilin	protein	122	28% helix, 32% strand	P78929

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A
LDA · Lauryl dimethylamine-N-oxide · additive · chains A

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

Compared structures

2I2Q · Fission Yeast cofilin · the same entry in another collection · chain A against A, TM-score 1.00
P78929 · AlphaFold monomer V2.0 prediction for cofilin (P78929) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P78929
Elsewhere: RCSB PDB 2I2Q · PDBe 2I2Q · UniProt P78929

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