Research workbench
G1 ORF67 / staphyloccus aureus sigmaa domain 4 complex
Analyse G1 ORF67 / staphyloccus aureus sigmaa domain 4 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G94
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase sigma factor rpod; ORF067
- UniProt
- P0A0J0, Q4Z9Y5
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase sigma factor rpod | protein | 62 | 71% helix, 0% strand | P0A0J0 |
| B | ORF067 | protein | 198 | 46% helix, 19% strand | Q4Z9Y5 |
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 | 95 | 0.44 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1334 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
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 P0A0J0
- Every structure of UniProt Q4Z9Y5
- Elsewhere: RCSB PDB 4G94 · PDBe 4G94 · UniProt P0A0J0 · UniProt Q4Z9Y5
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