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Crystal structure of alkaline mannanase from bacillus sp. strain jamb- 602: catalytic domain and its carbohydrate binding module

Analyse Crystal structure of alkaline mannanase from bacillus sp. strain jamb- 602… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WKY
Type: protein
Length: 446 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: Q4W8M3
Ligands: NA, CA, CL
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-mannanase (EC 3.2.1.78)	protein	446	26% helix, 32% strand	Q4W8M3

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A
CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.51	0.79	24	NA
2	180	0.44	0.74	31	empty
3	52	0.27	0.75	14	empty

Compared structures

1WKY · Crystal structure of alkaline mannanase from Bacillus sp. strain JAMB-602: catalytic… · 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 Q4W8M3
Elsewhere: RCSB PDB 1WKY · PDBe 1WKY · UniProt Q4W8M3

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