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The structure of GH113 beta-mannanase aamana from alicyclobacillus acidocaldarius in complex with manifg

Analyse The structure of GH113 beta-mannanase aamana from alicyclobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CD6
Type: protein
Length: 315 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,4-mannanase
EC: 3.2.1.78
UniProt: A5H1I6
Ligands: IFM, BMA
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-mannanase (EC 3.2.1.78)	protein	315	39% helix, 21% strand	A5H1I6

Ligands and binding sites

IFM · 5-hydroxymethyl-3,4-dihydroxypiperidine · ligand · chains A
BMA · beta-D-mannopyranose · sugar · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	206	0.52	0.77	18	IFM, BMA

Compared structures

4CD6 · The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in… · 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 A5H1I6
Elsewhere: RCSB PDB 4CD6 · PDBe 4CD6 · UniProt A5H1I6

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