MolNFT v1 · #176743 · protein

Structure of a novel beta-mannanase BAMAN113A with mannobiose, N236Y mutation.

7DW8 · Endo-beta-1,4-mannanase: “Structure of a novel beta-mannanase BAMAN113A with mannobiose, N236Y mutation.”. X-ray diffraction, 1 ligand (BMA), 3 pockets (best druggability 0.71). MolNFT v1 #176743 on GenesisL1: 3D structure, binding…

PDB: 7DW8
Type: protein
Length: 637 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,4-mannanase
UniProt: A0A140EH91
Ligands: BMA
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-mannanase	protein	323	40% helix, 20% strand	A0A140EH91
B	Endo-beta-1,4-mannanase	protein	314	41% helix, 20% strand	A0A140EH91

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · 4 copies · chains A, B

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	683	0.71	0.78	81	BMA
2	58	0.38	0.80	11	empty
3	63	0.37	0.79	12	empty

Interfaces

1 interface between chains.

A–B · 1015 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7DW8 · Structure of a novel beta-mannanase BaMan113A with mannobiose, N236Y mutation. · 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 A0A140EH91
Elsewhere: RCSB PDB 7DW8 · PDBe 7DW8 · UniProt A0A140EH91

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.