Research workbench
Crystal structure of STS042, a stand-alone ram module protein, from hyperthermophilic archaeon sulfolobus tokodaii STRAIN7.
Analyse Crystal structure of STS042, a stand-alone ram module protein, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZBC
- Type
- protein
- Length
- 648 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 83AA long hypothetical transcriptional regulator asnc
- UniProt
- Q975W5
- Ligands
- ILE
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | 83AA long hypothetical transcriptional regulator asnc | protein | 81 | 26% helix, 35% strand | Q975W5 |
Ligands and binding sites
- ILE · Isoleucine · ligand · 8 copies · chains A, D, C, B, E, F, H, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 582 | 0.65 | 0.77 | 50 | empty |
| 2 | 81 | 0.37 | 0.77 | 15 | empty |
| 3 | 82 | 0.37 | 0.76 | 26 | empty |
Interfaces
11 interfaces between chains.
- E–H · 1339 Ų buried · 23 hydrogen bonds · protein-protein
- F–G · 1335 Ų buried · 27 hydrogen bonds · protein-protein
- E–G · 541 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 541 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 539 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2ZBC · Crystal structure of STS042, a stand-alone RAM module protein, from hyperthermophilic… · the same entry in another collection · chain D against D, 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 Q975W5
- Elsewhere: RCSB PDB 2ZBC · PDBe 2ZBC · UniProt Q975W5
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