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Crystal structure of murine gsdmd

Analyse Crystal structure of murine gsdmd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N9N
Type: protein
Length: 766 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gasdermin-D
UniProt: Q9D8T2
Pockets: 9 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gasdermin-D	protein	378	39% helix, 16% strand	Q9D8T2
B	Gasdermin-D	protein	388	38% helix, 13% strand	Q9D8T2

Pockets

9 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	251	0.79	0.91	38	empty
2	645	0.79	0.84	108	empty
3	702	0.75	0.80	80	empty
4	756	0.75	0.80	69	empty
5	53	0.69	0.96	17	empty

Interfaces

1 interface between chains.

A–B · 606 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6N9N · Crystal structure of murine GSDMD · the same entry in another collection · chain A against A, TM-score 1.00
Q9D8T2 · AlphaFold monomer V2.0 prediction for gasdermin-D (Q9D8T2) · 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 Q9D8T2
Elsewhere: RCSB PDB 6N9N · PDBe 6N9N · UniProt Q9D8T2

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