Research workbench
Crystal structure of the metal-sensing transcriptional repressor czra from staphylococcus aureus in the apo-form
Analyse Crystal structure of the metal-sensing transcriptional repressor czra from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R1U
- Type
- protein
- Length
- 380 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Repressor protein
- UniProt
- O85142
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 64% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Repressor protein | protein | 94 | 64% helix, 14% strand | O85142 |
| B | Repressor protein | protein | 93 | 67% helix, 14% strand | O85142 |
| C | Repressor protein | protein | 98 | 63% helix, 12% strand | O85142 |
| D | Repressor protein | protein | 95 | 63% helix, 13% strand | O85142 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 558 | 0.71 | 0.80 | 67 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1754 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1557 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 432 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 427 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 162 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1R1U · Crystal structure of the metal-sensing transcriptional repressor CzrA from Staphylococcus… · 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 O85142
- Elsewhere: RCSB PDB 1R1U · PDBe 1R1U · UniProt O85142
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