Research workbench

Chimeric beta-glucosidase CEL1B-H13

Analyse Chimeric beta-glucosidase CEL1B-H13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KHT
Type: protein
Length: 1,431 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 1
UniProt: G0RIF5
Pockets: 14 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Glycoside hydrolase family 1	protein	477	39% helix, 16% strand	G0RIF5

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	724	0.73	0.79	56	empty
2	365	0.70	0.83	48	empty
3	338	0.70	0.83	36	empty
4	339	0.70	0.83	35	empty
5	289	0.69	0.83	34	empty

Interfaces

3 interfaces between chains.

B–C · 711 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 686 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 646 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6KHT · Chimeric beta-glucosidase Cel1b-H13 · 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 G0RIF5
Elsewhere: RCSB PDB 6KHT · PDBe 6KHT · UniProt G0RIF5

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