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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
2G4F
Type
protein
Length
604 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydrolase
EC
3.2.1.8
UniProt
Q7SI98
Pockets
2 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHydrolase (EC 3.2.1.8)protein30243% helix, 20% strandQ7SI98

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1830.330.7416empty
2610.290.7416empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2G4F · Structure of S.olivaceoviridis xylanase Q88A/R275A mutant · the same entry in another collection · chain A against A, TM-score 1.00

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