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Structure of the GH76A alpha-1,6-mannanase from salegentibacter sp. HEL1_6

Analyse Structure of the GH76A alpha-1,6-mannanase from salegentibacter sp. HEL1_6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SHD
Type
protein
Length
1,014 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-1,6-mannanase
Pockets
10 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CAlpha-1,6-mannanaseprotein33863% helix, 10% strand—

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12160.610.8125empty
21730.580.8226empty
32080.570.8026empty
41010.520.8325empty
51500.510.7924empty

Interfaces

2 interfaces between chains.

  • A–C · 475 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 465 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 6SHD · Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 · the same entry in another collection · chain A against A, TM-score 1.00

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