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Structure of beta-mannanase BAMAN113A with mannobiose

Analyse Structure of beta-mannanase BAMAN113A with mannobiose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DVJ
Type: protein
Length: 633 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: 4 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-mannanase	protein	310	39% helix, 19% strand	A0A140EH91
B	Endo-beta-1,4-mannanase	protein	323	39% helix, 19% strand	A0A140EH91

Ligands and binding sites

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

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

Pockets

4 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	808	0.73	0.78	85	BMA
2	57	0.38	0.80	10	empty
3	68	0.38	0.78	11	empty
4	70	0.31	0.74	10	empty

Interfaces

1 interface between chains.

A–B · 1012 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7DVJ · Structure of beta-mannanase BaMan113A with mannobiose · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt A0A140EH91
Elsewhere: RCSB PDB 7DVJ · PDBe 7DVJ · UniProt A0A140EH91

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