MolNFT v1 · #149306 · protein

Structure of an E336Q variant of the GH99 endo-alpha-mannanase from bacteroides xylanisolvens in complex with alpha-glc-1,3-1,2-anhydro- mannose hydrolyzed by enzyme

6FWO · Glycosyl hydrolase family 71: “Structure of an E336Q variant of the GH99 endo-alpha-mannanase from bacteroides xylanisolvens in complex with…”. X-ray diffraction, 2 ligands (M96, GLC), 1 pocket (best druggability 0.47). MolNFT v1…

PDB: 6FWO
Type: protein
Length: 342 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl hydrolase family 71
UniProt: D6D1V7
Ligands: M96, GLC
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyl hydrolase family 71	protein	342	33% helix, 17% strand	D6D1V7

Ligands and binding sites

M96 · (1~{S},2~{R},3~{S},4~{R},5~{R})-5-(hydroxymethyl) cyclohexane-1,2,3,4-tetrol · ligand · chains A
GLC · alpha-D-glucopyranose · sugar · chains A
ACT · Acetate ion · additive · 2 copies · 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	141	0.47	0.77	25	M96, GLC

Compared structures

6FWO · Structure of an E336Q variant of the GH99 endo-alpha-mannanase from Bacteroides… · 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 D6D1V7
Elsewhere: RCSB PDB 6FWO · PDBe 6FWO · UniProt D6D1V7

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