MolNFT v1 · #27937 · protein

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

1XYP · Endo-1,4-beta-xylanase II: “Structural comparison of two major endo-1,4-beta-xylanases from trichodrema reesei”. X-ray diffraction, 3 pockets (best druggability 0.52). MolNFT v1 #27937 on GenesisL1: 3D structure, binding sites and…

PDB: 1XYP
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 0.52

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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	268	0.52	0.75	35	empty
2	211	0.49	0.75	30	empty
3	95	0.38	0.76	27	empty

Interfaces

1 interface between chains.

A–B · 185 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cyclization).

Compared structures

1XYP · 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 0.99

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 1XYP · PDBe 1XYP · UniProt P36217

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