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Structure of S.OLIVACEOVIRIDIS xylanase Q88A/R275A mutant

Analyse Structure of S.OLIVACEOVIRIDIS xylanase Q88A/R275A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2G3I
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylanase
EC: 3.2.1.8
UniProt: Q7SI98
Ligands: PO4
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylanase (EC 3.2.1.8)	protein	303	42% helix, 20% strand	Q7SI98

Ligands and binding sites

PO4 · Phosphate ion · ion · 7 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	56	0.27	0.73	13	PO4

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2G3I · Structure of S.olivaceoviridis xylanase Q88A/R275A mutant · 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
Every structure of UniProt Q7SI98
Elsewhere: RCSB PDB 2G3I · PDBe 2G3I · UniProt Q7SI98

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