Research workbench

Computationally designed END0-1,4-BETA,XYLANASE

Analyse Computationally designed END0-1,4-BETA,XYLANASE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MFC
Type: protein
Length: 187 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase
EC: 3.2.1.8
UniProt: Q8GMV7
Ligands: SO4
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	187	5% helix, 62% strand	Q8GMV7

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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

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	176	0.49	0.76	21	SO4

Compared structures

3MFC · Computationally designed end0-1,4-beta,xylanase · 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 Q8GMV7
Elsewhere: RCSB PDB 3MFC · PDBe 3MFC · UniProt Q8GMV7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.