MolNFT v1 · #36538 · protein

An alkali thermostable F/10 xylanase from alkalophilic bacillus sp. ng-27

2F8Q · Alkaline thermostable endoxylanase: “An alkali thermostable F/10 xylanase from alkalophilic bacillus sp. ng-27”. X-ray diffraction, 1 ligand (MG), 3 pockets (best druggability 0.54). MolNFT v1 #36538 on GenesisL1: 3D structure…

PDB: 2F8Q
Type: protein
Length: 706 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alkaline thermostable endoxylanase
EC: 3.2.1.8
UniProt: O30700
Ligands: MG
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alkaline thermostable endoxylanase (EC 3.2.1.8)	protein	353	43% helix, 16% strand	O30700

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	151	0.54	0.81	29	empty
2	276	0.53	0.76	38	empty
3	165	0.52	0.79	29	empty

Interfaces

1 interface between chains.

A–B · 252 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2F8Q · An alkali thermostable F/10 xylanase from alkalophilic Bacillus sp. NG-27 · the same entry in another collection · chain B against B, 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 O30700
Elsewhere: RCSB PDB 2F8Q · PDBe 2F8Q · UniProt O30700

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