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Structural comparison of two major endo-1,4-beta-xylanases from trichodrema reesei

Analyse Structural comparison of two major endo-1,4-beta-xylanases from trichodrema… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XYN
Type: protein
Length: 178 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase I
EC: 3.2.1.8
UniProt: P36218
Ligands: CA
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 66% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase I (EC 3.2.1.8)	protein	178	6% helix, 66% strand	P36218

Ligands and binding sites

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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.51	0.78	26	empty

Compared structures

1XYN · Structural comparison of two major endo-1,4-beta-xylanases from trichodrema reesei · the same entry in another collection · chain A against A, TM-score 1.00
P36218 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 1 (P36218) · 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 P36218
Elsewhere: RCSB PDB 1XYN · PDBe 1XYN · UniProt P36218

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