MolNFT v1 · #24336 · protein

XYLANASE10C (mutant E385A) from cellvibrio japonicus in complex with xylopentaose

1US2 · Endo-beta-1,4-xylanase: “XYLANASE10C (mutant E385A) from cellvibrio japonicus in complex with xylopentaose”. X-ray diffraction, 1 ligand (XYP), 2 pockets (best druggability 0.61). MolNFT v1 #24336 on GenesisL1: 3D structure, binding…

PDB: 1US2
Type: protein
Length: 507 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,4-xylanase
EC: 3.2.1.8
UniProt: Q59675
Ligands: XYP
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-xylanase (EC 3.2.1.8)	protein	507	31% helix, 26% strand	Q59675

Ligands and binding sites

XYP · beta-D-xylopyranose · sugar · 8 copies · chains A

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

Pockets

2 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	309	0.61	0.79	46	XYP
2	65	0.29	0.74	17	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1US2 · Xylanase10C (mutant E385A) from Cellvibrio japonicus in complex with xylopentaose · the same entry in another collection · chain A against A, TM-score 1.00
Q59675 · AlphaFold monomer V2.0 prediction for endo-beta-1,4-xylanase XYN10C (Q59675) · 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 Q59675
Elsewhere: RCSB PDB 1US2 · PDBe 1US2 · UniProt Q59675

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