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Structural basis for mutation-induced destabilization of profilin 1 in als

Analyse Structural basis for mutation-induced destabilization of profilin 1 in als in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4X1M
Type: protein
Length: 128 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Profilin-1
UniProt: P07737

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Profilin-1	protein	128	27% helix, 34% strand	P07737

Compared structures

4X1M · Structural basis for mutation-induced destabilization of Profilin 1 in ALS · the same entry in another collection · chain A against A, TM-score 1.00
P07737 · AlphaFold monomer V2.0 prediction for profilin-1 (P07737) · 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 P07737
Elsewhere: RCSB PDB 4X1M · PDBe 4X1M · UniProt P07737

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