Research workbench

N184K pathological variant of gelsolin domain 2 (trigonal form)

Analyse N184K pathological variant of gelsolin domain 2 (trigonal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FAE
Type: protein
Length: 108 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gelsolin
UniProt: P06396
Ligands: CA, SO4, CL
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gelsolin	protein	108	26% helix, 26% strand	P06396

Ligands and binding sites

CA · Calcium ion · metal · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
CL · Chloride ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.34	0.76	13	PEG

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5FAE · N184K pathological variant of gelsolin domain 2 (trigonal form) · the same entry in another collection · chain A against A, TM-score 1.00
P06396 · AlphaFold monomer V2.0 prediction for gelsolin (P06396) · a predicted model of the same protein · chain A against A, TM-score 0.82

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 P06396
Elsewhere: RCSB PDB 5FAE · PDBe 5FAE · UniProt P06396

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