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Crystal structure of endo-beta-1,4-xylanase from the alkaliphilic bacillus sp. SN5

Analyse Crystal structure of endo-beta-1,4-xylanase from the alkaliphilic bacillus sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IXL
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylanase
EC: 3.2.1.8
Ligands: SO4
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylanase (EC 3.2.1.8)	protein	206	7% helix, 64% strand	—
B	Xylanase (EC 3.2.1.8)	protein	206	7% helix, 62% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

3 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	274	0.53	0.75	31	empty
2	220	0.49	0.75	29	empty
3	156	0.43	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 370 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

4IXL · Crystal structure of endo-beta-1,4-xylanase from the alkaliphilic Bacillus sp. SN5 · the same entry in another collection · 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
Elsewhere: RCSB PDB 4IXL · PDBe 4IXL

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