MolNFT v1 · #189176 · protein
Structure of horcolin native form
7V4Z: “Structure of horcolin native form”. X-ray diffraction, 14 pockets (best druggability 0.85). MolNFT v1 #189176 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7V4Z
- Type
- protein
- Length
- 1,721 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Horcolin
- UniProt
- Q5U9T2
- Pockets
- 14 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 67% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, G, J | Horcolin | protein | 144 | 0% helix, 66% strand | Q5U9T2 |
| B, E, F, H, I, K, L | Horcolin | protein | 143 | 0% helix, 67% strand | Q5U9T2 |
Ligands and binding sites
- GOL · Glycerol · additive · 26 copies · chains A, C, E, B, G, D, F, H, I, J, K, L
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, C, K
- PEG · Di(hydroxyethyl)ether · additive · chains C, B, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 985 | 0.85 | 0.86 | 107 | empty |
| 2 | 930 | 0.85 | 0.86 | 108 | empty |
| 3 | 1084 | 0.71 | 0.75 | 111 | GOL, PEG |
| 4 | 50 | 0.68 | 0.97 | 24 | empty |
| 5 | 483 | 0.64 | 0.76 | 64 | empty |
Interfaces
29 interfaces between chains.
- K–L · 837 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 832 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 822 Ų buried · 7 hydrogen bonds · protein-protein
- I–J · 818 Ų buried · 8 hydrogen bonds · protein-protein
- E–F · 816 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7V4Z · Structure of Horcolin native form · the same entry in another collection · chain L against L, 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 Q5U9T2
- Elsewhere: RCSB PDB 7V4Z · PDBe 7V4Z · UniProt Q5U9T2
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