MolNFT v1 · #9608 · protein

0.89A ultra high resolution structure of a thermostable xylanase from thermoascus aurantiacus

1I1W · Endo-1,4-beta-xylanase: “0.89A ultra high resolution structure of a thermostable xylanase from thermoascus aurantiacus”. X-ray diffraction, 2 ligands (ACN, UNX). MolNFT v1 #9608 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1I1W
Type: protein
Length: 303 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: P23360
Ligands: ACN, UNX

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	303	43% helix, 19% strand	P23360

Ligands and binding sites

ACN · Acetone · ligand · chains A
UNX · Unknown atom or ion · ion · 13 copies · chains A
GOL · Glycerol · additive · 6 copies · chains A
EOH · Ethanol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, cyclization).

Compared structures

1I1W · 0.89A Ultra high resolution structure of a Thermostable Xylanase from Thermoascus… · the same entry in another collection · chain A against A, TM-score 1.00
P23360 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P23360) · 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 P23360
Elsewhere: RCSB PDB 1I1W · PDBe 1I1W · UniProt P23360

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