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Crystal structure of weissella viridescens femx form II

Analyse Crystal structure of weissella viridescens femx form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XIX
Type: protein
Length: 335 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Femx
EC: 2.3.2.10
UniProt: Q9EY50
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 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

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	536	0.64	0.76	59	empty
2	124	0.54	0.82	23	empty
3	68	0.30	0.74	18	empty

Compared structures

1XIX · Crystal Structure of Weissella viridescens FemX Form II · 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 1XIX · PDBe 1XIX · UniProt Q9EY50

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