Research workbench

Catalytic core of xylanase a E246C mutant

Analyse Catalytic core of xylanase a E246C mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XYS
Type: protein
Length: 690 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylanase a
EC: 3.2.1.8
UniProt: P14768
Ligands: CA

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Xylanase a (EC 3.2.1.8)	protein	345	0% helix, 0% strand	P14768

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 153 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1XYS · Catalytic core of xylanase a E246C mutant · the same entry in another collection · chain A against A, TM-score 1.00
P14768 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase a (P14768) · 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 P14768
Elsewhere: RCSB PDB 1XYS · PDBe 1XYS · UniProt P14768

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.