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2.1 Angstrom resolution crystal structure of S-layer domain-containing protein (residues 221-444) from Clostridium thermocellum ATCC 27405
Analyse 2.1 Angstrom resolution crystal structure of S-layer domain-containing protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QVS
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Ruminiclostridium thermocellum ATCC 27405
- Molecule
- S-layer domain-containing protein
- UniProt
- A3DIC9
- Ligands
- NA, CL
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 6% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-layer domain-containing protein | protein | 217 | 6% helix, 27% strand | A3DIC9 |
Ligands and binding sites
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 | 823 | 0.71 | 0.77 | 58 | empty |
| 2 | 216 | 0.50 | 0.75 | 29 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4QVS · 2.1 ångström resolution crystal structure of S-layer domain-containing protein (residues… · 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 A3DIC9
- Elsewhere: RCSB PDB 4QVS · PDBe 4QVS · UniProt A3DIC9
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