Research workbench
Structure of P. aeruginosa ATCC27853 nucc, caaa-bound form
Analyse Structure of P. aeruginosa ATCC27853 nucc, caaa-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q1H
- Type
- protein + RNA
- Length
- 1,445 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterial protein orf C62; RNA (5'-R(P*AP*AP*A)-3')
- UniProt
- Q8GQ48
- Pockets
- 20 · best druggability 0.61
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F | Bacterial protein orf C62 | protein | 240 | 37% helix, 27% strand | Q8GQ48 |
| D, H | RNA (5'-R(P*AP*AP*A)-3') | rna | 3 | — | — |
| G | Bacterial protein orf C62 | protein | 239 | 38% helix, 27% strand | Q8GQ48 |
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 329 | 0.61 | 0.78 | 32 | empty |
| 2 | 332 | 0.61 | 0.78 | 34 | empty |
| 3 | 502 | 0.60 | 0.74 | 60 | empty |
| 4 | 311 | 0.60 | 0.78 | 38 | empty |
| 5 | 460 | 0.57 | 0.74 | 56 | empty |
Interfaces
18 interfaces between chains.
- B–C · 1525 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 1523 Ų buried · 13 hydrogen bonds · protein-protein
- F–G · 1514 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1514 Ų buried · 12 hydrogen bonds · protein-protein
- E–G · 1513 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6Q1H · Structure of P. aeruginosa ATCC27853 NucC, cAAA-bound form · 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 Q8GQ48
- Elsewhere: RCSB PDB 6Q1H · PDBe 6Q1H · UniProt Q8GQ48
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