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Crystal Structure of Weissella viridescens FemX (K36M) Mutant

Analyse Crystal Structure of Weissella viridescens FemX (K36M) Mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XE4
Type: protein
Length: 335 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.95
Source: Weissella viridescens
Molecule: FemX
EC: 2.3.2.10
UniProt: Q9EY50
Ligands: MG
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · resolution 1.95 · 1 distinct chain · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FemX (EC 2.3.2.10)	protein	335	37% helix, 27% strand	Q9EY50

Ligands and binding sites

MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	578	0.66	0.76	60	empty
2	116	0.55	0.83	25	empty
3	60	0.29	0.74	16	empty

Compared structures

1XE4 · Crystal structure of weissella viridescens femx (K36M) mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q9EY50 · AlphaFold monomer V2.0 prediction for udp-N- acetylmuramoylpentapeptide-lysine… · a predicted model of the same protein · 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 Q9EY50
Elsewhere: RCSB PDB 1XE4 · PDBe 1XE4 · UniProt Q9EY50

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