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C-terminal half of gelsolin soaked in egta at pH 8

Analyse C-terminal half of gelsolin soaked in egta at pH 8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FH4
Type: protein
Length: 944 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gelsolin
UniProt: P06396
Pockets: 14 · best druggability 0.61

Structure

x-ray diffraction · 3 distinct chains · 24% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gelsolin	protein	307	22% helix, 27% strand	P06396
B	Gelsolin	protein	319	25% helix, 29% strand	P06396
C	Gelsolin	protein	318	23% helix, 29% strand	P06396

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.61	0.93	19	empty
2	217	0.60	0.81	32	empty
3	215	0.59	0.81	36	empty
4	159	0.55	0.81	32	empty
5	197	0.54	0.79	23	empty

Interfaces

2 interfaces between chains.

A–B · 393 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 69 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2FH4 · C-terminal half of gelsolin soaked in EGTA at pH 8 · 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 0.64

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 2FH4 · PDBe 2FH4 · UniProt P06396

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