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Crystal structure of UFM1 in complex with UBA5
Analyse Crystal structure of UFM1 in complex with UBA5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HKH
- Type
- protein
- Length
- 174 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-fold modifier 1; Asp-asn-glu-TRP-gly-ile-glu-leu-val
- UniProt
- P61960
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 3 distinct chains · 22% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-fold modifier 1 | protein | 86 | 22% helix, 31% strand | P61960 |
| B | Asp-asn-glu-TRP-gly-ile-glu-leu-val | protein | 9 | 0% helix, 22% strand | — |
| C | Ubiquitin-fold modifier 1 | protein | 79 | 25% helix, 33% strand | P61960 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.45 | 0.81 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 453 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 296 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 229 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 P61960
- Elsewhere: RCSB PDB 5HKH · PDBe 5HKH · UniProt P61960
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