Research workbench
Structure of XL5-ligated HRPN13 pru domain
Analyse Structure of XL5-ligated HRPN13 pru domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KXI
- Type
- protein
- Length
- 110 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasomal ubiquitin receptor ADRM1
- UniProt
- Q16186
- Ligands
- XAY
- Pockets
- 1 · best druggability 0.28
Structure
solution nmr · 1 distinct chain · 12% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteasomal ubiquitin receptor ADRM1 | protein | 110 | 12% helix, 48% strand | Q16186 |
Ligands and binding sites
- XAY · 2-{[(2S)-2-cyano-3-{3-[(4-methylbenzene-1-carbonyl) amino]phenyl}propanoyl]amino}benzoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 55 | 0.28 | 0.73 | 14 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 Q16186
- Elsewhere: RCSB PDB 7KXI · PDBe 7KXI · UniProt Q16186
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