MolNFT v1 · #144597 · protein

Crystal structure of the acid-base mutant (E477A) of the GH2 exo-beta- mannanase from xanthomonas axonopodis pv. citri

6BYI · Beta-mannosidase: “Crystal structure of the acid-base mutant (E477A) of the GH2 exo-beta- mannanase from xanthomonas axonopodis…”. X-ray diffraction, 1 ligand (BMA), 18 pockets (best druggability 0.77). MolNFT v1 #144597 on…

PDB: 6BYI
Type: protein
Length: 1,718 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-mannosidase
UniProt: Q8PI23
Ligands: BMA
Pockets: 18 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-mannosidase	protein	859	26% helix, 35% strand	Q8PI23

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · 5 copies · chains A, B

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

Pockets

18 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	563	0.77	0.84	54	empty
2	542	0.77	0.84	52	empty
3	99	0.76	0.97	29	empty
4	650	0.73	0.80	75	BMA
5	664	0.70	0.78	76	empty

Interfaces

1 interface between chains.

A–B · 1671 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

6BYI · Crystal structure of the acid-base mutant (E477A) of the GH2 exo-beta-mannanase from… · 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 Q8PI23
Elsewhere: RCSB PDB 6BYI · PDBe 6BYI · UniProt Q8PI23

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