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Structural studies on the mobility in the active site of the thermoascus aurantiacus xylanase I

Analyse Structural studies on the mobility in the active site of the thermoascus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K6A
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylanase I
EC: 3.2.1.8
UniProt: P23360
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylanase I (EC 3.2.1.8)	protein	302	44% helix, 19% strand	P23360

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.35	0.79	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1K6A · Structural studies on the mobility in the active site of the Thermoascus aurantiacus… · 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 1K6A · PDBe 1K6A · UniProt P23360

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