MolNFT v1 · #185580 · protein
A de novo designed hetero-dimeric antiparallel coiled coil apcc-di- AB_VAR
7Q1S · Apcc-di-B_VAR: “A de novo designed hetero-dimeric antiparallel coiled coil apcc-di- AB_VAR”. X-ray diffraction, 1 ligand (ACE), 4 pockets (best druggability 0.72). MolNFT v1 #185580 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7Q1S
- Type
- protein
- Length
- 407 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apcc-di-B_VAR; Apcc-di-A_VAR
- Ligands
- ACE
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 8 distinct chains · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, J, N | Apcc-di-B_VAR | protein | 30 | 90% helix, 0% strand | — |
| E, M, A | Apcc-di-A_VAR | protein | 30 | 87% helix, 0% strand | — |
| L, B | Apcc-di-B_VAR | protein | 29 | 90% helix, 0% strand | — |
| K | Apcc-di-A_VAR | protein | 27 | 85% helix, 0% strand | — |
| I, G | Apcc-di-A_VAR | protein | 28 | 86% helix, 0% strand | — |
| D | Apcc-di-B_VAR | protein | 29 | 90% helix, 0% strand | — |
| C | Apcc-di-A_VAR | protein | 29 | 90% helix, 0% strand | — |
| H | Apcc-di-B_VAR | protein | 28 | 93% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains F, M, L, C, N, D, A
- EDO · 1,2-ethanediol · additive · 5 copies · chains F, E, D, L, I, C, M, N, H, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 539 | 0.72 | 0.81 | 46 | EDO |
| 2 | 460 | 0.66 | 0.78 | 51 | empty |
| 3 | 73 | 0.32 | 0.74 | 19 | EDO |
| 4 | 68 | 0.29 | 0.73 | 12 | empty |
Interfaces
38 interfaces between chains.
- L–I · 915 Ų buried · 13 hydrogen bonds · protein-protein
- M–N · 912 Ų buried · 6 hydrogen bonds · protein-protein
- D–C · 895 Ų buried · 6 hydrogen bonds · protein-protein
- L–K · 892 Ų buried · 4 hydrogen bonds · protein-protein
- F–E · 880 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (covalent ligand).
Compared structures
- 7Q1S · A de novo designed hetero-dimeric antiparallel coiled coil apCC-Di-AB_var · the same entry in another collection · chain F against F, 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
- Elsewhere: RCSB PDB 7Q1S · PDBe 7Q1S
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.