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Carbohydrate binding module (CBM6CM-2) from cellvibrio mixtus lichenase 5A in complex with cellotriose

Analyse Carbohydrate binding module (CBM6CM-2) from cellvibrio mixtus lichenase 5A in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UYY
Type: protein
Length: 262 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulase B
UniProt: O07653
Ligands: BGC, CA
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cellulase B	protein	131	0% helix, 62% strand	O07653

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 7 copies · chains A, B
CA · Calcium ion · metal · 4 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	119	0.36	0.73	22	BGC
2	74	0.33	0.75	17	BGC

Interfaces

1 interface between chains.

A–B · 444 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1UYY · Carbohydrate binding module (CBM6cm-2) from Cellvibrio mixtus lichenase 5A in complex… · 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 O07653
Elsewhere: RCSB PDB 1UYY · PDBe 1UYY · UniProt O07653

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