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Catalytic domain of bacillus sp. jamb-750 GH26 endo-beta-1,4-mannanase

Analyse Catalytic domain of bacillus sp. jamb-750 GH26 endo-beta-1,4-mannanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4YN5
Type: protein
Length: 391 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mannan endo-1,4-beta-mannosidase
UniProt: Q2ACI1
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mannan endo-1,4-beta-mannosidase	protein	391	34% helix, 15% strand	Q2ACI1

Ligands and binding sites

CAC · Cacodylate ion · additive · 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	210	0.47	0.74	27	CAC

Compared structures

4YN5 · Catalytic domain of Bacillus sp. JAMB-750 GH26 Endo-beta-1,4-mannanase · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q2ACI1
Elsewhere: RCSB PDB 4YN5 · PDBe 4YN5 · UniProt Q2ACI1

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