MolNFT v1 · #172797 · protein
Orf virus apoptosis inhibitor ORFV125
7ADT: “Orf virus apoptosis inhibitor ORFV125”. X-ray diffraction, 1 ligand (MG), 5 pockets (best druggability 0.80). MolNFT v1 #172797 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7ADT
- Type
- protein
- Length
- 310 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apoptosis inhibitor; Apoptosis regulator bax
- UniProt
- A0A0R8HV90, Q07812
- Ligands
- MG
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apoptosis inhibitor | protein | 130 | 79% helix, 0% strand | A0A0R8HV90 |
| U | Apoptosis regulator bax | protein | 23 | 83% helix, 0% strand | Q07812 |
| B | Apoptosis inhibitor | protein | 131 | 81% helix, 0% strand | A0A0R8HV90 |
| C | Apoptosis regulator bax | protein | 26 | 81% helix, 0% strand | Q07812 |
Ligands and binding sites
- MG · Magnesium ion · metal · 41 copies · chains A, B, U, C
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.80 | 0.97 | 21 | EDO |
| 2 | 135 | 0.40 | 0.74 | 19 | empty |
| 3 | 84 | 0.36 | 0.76 | 17 | MG |
| 4 | 94 | 0.35 | 0.73 | 18 | MG |
| 5 | 60 | 0.31 | 0.74 | 9 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2835 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 955 Ų buried · 8 hydrogen bonds · protein-protein
- A–U · 840 Ų buried · 6 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 A0A0R8HV90
- Every structure of UniProt Q07812
- Elsewhere: RCSB PDB 7ADT · PDBe 7ADT · UniProt A0A0R8HV90 · UniProt Q07812
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