Research workbench
GH124 cellulase from ruminiclostridium thermocellum in complex with mn and fructosylated cellopentaose
Analyse GH124 cellulase from ruminiclostridium thermocellum in complex with mn and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G1I
- Type
- protein
- Length
- 420 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolase
- UniProt
- A3DCJ4
- Ligands
- BGC, FRU, MN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glycosyl hydrolase | protein | 210 | 55% helix, 4% strand | A3DCJ4 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 14 copies · chains A, B
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- MLA · Malonic acid · additive · 2 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 922 | 0.68 | 0.74 | 84 | BGC, FRU |
| 2 | 113 | 0.42 | 0.77 | 24 | FRU, BGC |
Interfaces
1 interface between chains.
- A–B · 96 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6G1I · GH124 cellulase from Ruminiclostridium thermocellum in complex with Mn and fructosylated… · 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 A3DCJ4
- Elsewhere: RCSB PDB 6G1I · PDBe 6G1I · UniProt A3DCJ4
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