MolNFT v1 · #94152 · protein
Crystal structure of eukaryotic hslv from trypanosoma brucei
4HNZ · Hslvu complex proteolytic subunit, putative: “Crystal structure of eukaryotic hslv from trypanosoma brucei”. X-ray diffraction, 1 ligand (MG), 20 pockets (best druggability 0.77). MolNFT v1 #94152 on GenesisL1: 3D structure, binding…
- PDB
- 4HNZ
- Type
- protein
- Length
- 2,088 residues
- Chains
- 12
- 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
- 20 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Hslvu complex proteolytic subunit, putative (EC 3.4.25.-) | protein | 174 | 35% helix, 32% strand | Q383Q5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1081 | 0.77 | 0.79 | 136 | empty |
| 2 | 408 | 0.70 | 0.81 | 67 | empty |
| 3 | 371 | 0.66 | 0.80 | 45 | MG |
| 4 | 373 | 0.65 | 0.80 | 44 | MG |
| 5 | 322 | 0.65 | 0.81 | 40 | MG |
Interfaces
24 interfaces between chains.
- G–H · 836 Ų buried · 18 hydrogen bonds · protein-protein
- I–J · 828 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 827 Ų buried · 18 hydrogen bonds · protein-protein
- G–L · 827 Ų buried · 19 hydrogen bonds · protein-protein
- J–K · 826 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 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 4HNZ · PDBe 4HNZ · UniProt Q383Q5
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