Research workbench
GH124 cellulase from ruminiclostridium thermocellum in complex with mn and cellotriose
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
- 6G1G
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolase
- UniProt
- A3DCJ4
- Ligands
- BGC, MN
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl hydrolase | protein | 211 | 55% helix, 4% strand | A3DCJ4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.41 | 0.76 | 25 | BGC |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 6G1G · GH124 cellulase from Ruminiclostridium thermocellum in complex with Mn and cellotriose · 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 6G1G · PDBe 6G1G · UniProt A3DCJ4
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