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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: 1ENX
Type: protein
Length: 380 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase II
EC: 3.2.1.8
UniProt: P36217
Pockets: 3 · best druggability 0.53

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endo-1,4-beta-xylanase II (EC 3.2.1.8)	protein	190	5% helix, 62% strand	P36217

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	287	0.53	0.75	36	empty
2	248	0.52	0.75	32	empty
3	88	0.36	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 188 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cyclization).

Compared structures

1ENX · 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
P36217 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 2 (P36217) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P36217
Elsewhere: RCSB PDB 1ENX · PDBe 1ENX · UniProt P36217

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