Research workbench
Structure of P. aeruginosa ATCC27853 CDND:HORMA2:PEPTIDE 1 complex
Analyse Structure of P. aeruginosa ATCC27853 CDND:HORMA2:PEPTIDE 1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P8U
- Type
- protein
- Length
- 472 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleotidyltransferase; Horma domain containing protein; Peptide 1
- UniProt
- A0A080VY32, Q8GQ50
- Ligands
- MG
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotidyltransferase | protein | 300 | 50% helix, 13% strand | A0A080VY32 |
| B | Horma domain containing protein | protein | 165 | 31% helix, 34% strand | Q8GQ50 |
| C | Peptide 1 | protein | 7 | 0% helix, 71% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 585 | 0.79 | 0.85 | 54 | MG |
| 2 | 111 | 0.41 | 0.76 | 20 | empty |
Interfaces
2 interfaces between chains.
- A–B · 987 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 725 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6P8U · Structure of P. aeruginosa ATCC27853 CdnD:HORMA2:Peptide 1 complex · 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 A0A080VY32
- Every structure of UniProt Q8GQ50
- Elsewhere: RCSB PDB 6P8U · PDBe 6P8U · UniProt A0A080VY32 · UniProt Q8GQ50
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