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Structure of a novel beta-mannanase BAMAN113A from bacillus sp. N16-5, N236Y mutation.

Analyse Structure of a novel beta-mannanase BAMAN113A from bacillus sp. N16-5, N236Y… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DVZ
Type
protein
Length
640 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endo-beta-1,4-mannanase
UniProt
A0A140EH91
Pockets
4 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndo-beta-1,4-mannanaseprotein32640% helix, 18% strandA0A140EH91
BEndo-beta-1,4-mannanaseprotein31441% helix, 19% strandA0A140EH91

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14280.640.7747empty
24010.630.7752empty
3620.390.8012empty
4540.390.8112empty

Interfaces

1 interface between chains.

  • A–B · 1009 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 7DVZ · Structure of a novel beta-mannanase BaMan113A from Bacillus sp. N16-5, N236Y mutation. · the same entry in another collection · chain A against A, TM-score 1.00

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