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Crystal structure of flim middle domain from H. pylori

Analyse Crystal structure of flim middle domain from H. pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GC8
Type: protein
Length: 532 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar motor switch protein
UniProt: O25675
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar motor switch protein	protein	184	39% helix, 29% strand	O25675
B, C	Flagellar motor switch protein	protein	174	41% helix, 30% strand	O25675

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	313	0.59	0.78	33	empty
2	288	0.51	0.74	33	empty
3	53	0.33	0.77	16	empty

Interfaces

3 interfaces between chains.

B–C · 322 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 232 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 21 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4GC8 · Crystal structure of FliM middle domain from H. pylori · the same entry in another collection · chain A against A, TM-score 1.00

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 O25675
Elsewhere: RCSB PDB 4GC8 · PDBe 4GC8 · UniProt O25675

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