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Crystal structure of femx

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

PDB: 6SNR
Type: protein
Length: 402 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipid II:GLYCINE glycyltransferase
EC: 2.3.2.16
UniProt: P0C1Q0
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipid II:GLYCINE glycyltransferase (EC 2.3.2.16)	protein	402	49% helix, 23% strand	P0C1Q0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	710	0.67	0.75	63	empty
2	74	0.37	0.77	17	empty
3	98	0.35	0.74	26	empty

Compared structures

6SNR · Crystal structure of FemX · the same entry in another collection · chain A against A, TM-score 1.00
P0C1Q0 · AlphaFold monomer V2.0 prediction for lipid II:GLYCINE glycyltransferase (P0C1Q0) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P0C1Q0
Elsewhere: RCSB PDB 6SNR · PDBe 6SNR · UniProt P0C1Q0

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