Research workbench
De novo phasing of a hamp-complex using an improved arcimboldo method
Analyse De novo phasing of a hamp-complex using an improved arcimboldo method in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GN0
- Type
- protein
- Length
- 412 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hamp domain of AF1503
- UniProt
- O28769
- Ligands
- MG
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 3 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hamp domain of AF1503 | protein | 105 | 76% helix, 0% strand | O28769 |
| B | Hamp domain of AF1503 | protein | 103 | 79% helix, 0% strand | O28769 |
| C, D | Hamp domain of AF1503 | protein | 102 | 79% helix, 0% strand | O28769 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.41 | 0.77 | 21 | empty |
| 2 | 51 | 0.27 | 0.74 | 15 | empty |
Interfaces
2 interfaces between chains.
- B–D · 1298 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 1274 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4GN0 · De novo phasing of a Hamp-complex using an improved Arcimboldo method · 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 O28769
- Elsewhere: RCSB PDB 4GN0 · PDBe 4GN0 · UniProt O28769
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