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Crystal structures of mutant endo-beta-1,4-xylanase II complexed with substrate (1.15 a) and products (1.6 a)

Analyse Crystal structures of mutant endo-beta-1,4-xylanase II complexed with substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HKL
Type: protein
Length: 189 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase 2
EC: 3.2.1.8
UniProt: P36217
Ligands: IOD
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 61% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase 2 (EC 3.2.1.8)	protein	189	5% helix, 61% strand	P36217

Ligands and binding sites

IOD · Iodide ion · ion · 4 copies · chains A

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

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	180	0.48	0.76	29	empty

Compared structures

4HKL · Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A)… · 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 4HKL · PDBe 4HKL · UniProt P36217

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