Research workbench
Crystal structure of the pseudomonas capeferrum anti-sigma regulator pupr C-terminal cell-surface signaling domain in complex with the outer membrane transporter pupb N-terminal signaling domain
Analyse Crystal structure of the pseudomonas capeferrum anti-sigma regulator pupr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OVK
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Siderophore-interacting protein; Ferric-pseudobactin BN7/BN8 receptor
- UniProt
- A0A084CH09, A0A084CH10
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | Siderophore-interacting protein | protein | 213 | 13% helix, 53% strand | A0A084CH09 |
| B | Ferric-pseudobactin BN7/BN8 receptor | protein | 81 | 30% helix, 37% strand | A0A084CH10 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · 2 copies · chains R
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 | 410 | 0.65 | 0.79 | 40 | empty |
| 2 | 104 | 0.37 | 0.75 | 25 | empty |
| 3 | 52 | 0.27 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- R–B · 762 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6OVK · Crystal Structure of the Pseudomonas capeferrum Anti-sigma Regulator PupR C-terminal… · the same entry in another collection · chain R against R, 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 A0A084CH09
- Every structure of UniProt A0A084CH10
- Elsewhere: RCSB PDB 6OVK · PDBe 6OVK · UniProt A0A084CH09 · UniProt A0A084CH10
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