MolNFT v1 · #94160 · protein
Crystal structure of eukaryotic hslv from trypanosoma brucei
4HO7 · Hslvu complex proteolytic subunit, putative: “Crystal structure of eukaryotic hslv from trypanosoma brucei”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.69). MolNFT v1 #94160 on GenesisL1: 3D structure, binding…
- PDB
- 4HO7
- Type
- protein
- Length
- 519 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hslvu complex proteolytic subunit, putative
- EC
- 3.4.25.-
- UniProt
- Q383Q5
- Ligands
- MG
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Hslvu complex proteolytic subunit, putative (EC 3.4.25.-) | protein | 173 | 35% helix, 31% strand | Q383Q5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, B, 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 756 | 0.69 | 0.76 | 88 | empty |
| 2 | 224 | 0.48 | 0.74 | 36 | empty |
Interfaces
3 interfaces between chains.
- A–C · 848 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 842 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 14 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4HO7 · Crystal structure of eukaryotic HslV from Trypanosoma brucei · the same entry in another collection · chain A against A, TM-score 1.00
- Q383Q5 · AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (Q383Q5) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q383Q5
- Elsewhere: RCSB PDB 4HO7 · PDBe 4HO7 · UniProt Q383Q5
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