Research workbench
Tetrameric cryo-EM arna
Analyse Tetrameric cryo-EM arna in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PIK
- Type
- protein
- Length
- 2,484 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional polymyxin resistance protein arna; Udp-4-amino-4-deoxy-L-arabinose…
- EC
- 2.1.2.13, 1.1.1.305
- UniProt
- A0A3W2RQG2, A0A479JW67
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Bifunctional polymyxin resistance protein arna (EC 2.1.2.13, 1.1.1.305) | protein | 291 | 31% helix, 29% strand | A0A3W2RQG2 |
| E, F, G, H | Udp-4-amino-4-deoxy-L-arabinose formyltransferase | protein | 330 | 45% helix, 18% strand | A0A479JW67 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 540 | 0.75 | 0.83 | 76 | empty |
| 2 | 665 | 0.73 | 0.80 | 59 | empty |
| 3 | 638 | 0.73 | 0.80 | 51 | empty |
| 4 | 564 | 0.72 | 0.81 | 46 | empty |
| 5 | 604 | 0.72 | 0.80 | 47 | empty |
Interfaces
15 interfaces between chains.
- F–G · 1048 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 696 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 666 Ų buried · 4 hydrogen bonds · protein-protein
- E–F · 269 Ų buried · 0 hydrogen bonds · protein-protein
- G–H · 269 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6PIK · Tetrameric cryo-EM ArnA · 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 A0A3W2RQG2
- Every structure of UniProt A0A479JW67
- Elsewhere: RCSB PDB 6PIK · PDBe 6PIK · UniProt A0A3W2RQG2 · UniProt A0A479JW67
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