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Engineered CBM X-2 L110F in complex with branched carbohydrate XXXG.

Analyse Engineered CBM X-2 L110F in complex with branched carbohydrate XXXG. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DPN
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction, neutron diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.6,1.606
Source: Rhodothermus marinus
Molecule: Xylanase
UniProt: Q7WTN6
Ligands: BGC, XYS, CA
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction, neutron diffraction · resolution 1.6,1.606 · 1 distinct chain · 4% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylanase	protein	166	4% helix, 48% strand	Q7WTN6

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
XYS · alpha-D-xylopyranose · sugar · 3 copies · chains A
CA · Calcium ion · metal · 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	76	0.36	0.76	15	XYS

Compared structures

5DPN · Engineered cbm X-2 L110F in complex with branched carbohydrate xxxg. · 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 Q7WTN6
Elsewhere: RCSB PDB 5DPN · PDBe 5DPN · UniProt Q7WTN6

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