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Improved ligand discovery using micro-beam data collection at the edge of protein crystals

Analyse Improved ligand discovery using micro-beam data collection at the edge of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MGU
Type: protein
Length: 190 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: B2CZF9
Ligands: ARG, NA
Pockets: 1 · best druggability 0.50

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	190	5% helix, 62% strand	B2CZF9

Ligands and binding sites

ARG · Arginine · ligand · chains A
NA · Sodium ion · metal · 5 copies · chains A
EDO · 1,2-ethanediol · additive · 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	201	0.50	0.76	32	ARG

Modifications

Observed in the structure: 1 modified (cyclization).

Compared structures

7MGU · Improved ligand discovery using micro-beam data collection at the edge of protein crystals · 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 B2CZF9
Elsewhere: RCSB PDB 7MGU · PDBe 7MGU · UniProt B2CZF9

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