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High resolution structure of the major periplasmic domain from the cell shape-determining filament mrec (monoclinic form)

Analyse High resolution structure of the major periplasmic domain from the cell… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QF5
Type: protein
Length: 158 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell shape determining protein mrec
UniProt: Q8DMY2
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell shape determining protein mrec	protein	158	2% helix, 58% strand	Q8DMY2

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	55	0.42	0.82	17	empty

Compared structures

2QF5 · High resolution structure of the major periplasmic domain from the cell shape-determining… · the same entry in another collection · chain A against A, TM-score 1.00
Q8DMY2 · AlphaFold monomer V2.0 prediction for cell shape-determining protein mrec (Q8DMY2) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q8DMY2
Elsewhere: RCSB PDB 2QF5 · PDBe 2QF5 · UniProt Q8DMY2

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