Research workbench
Crystal structure of the human arc N-lobe bound to repeat 4 from gkap
Analyse Crystal structure of the human arc N-lobe bound to repeat 4 from gkap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TNQ
- Type
- protein
- Length
- 230 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Activity-regulated cytoskeleton-associated protein; Chains: B,D,F
- UniProt
- Q7LC44
- Ligands
- ACE
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 6 distinct chains · 65% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Activity-regulated cytoskeleton-associated protein | protein | 67 | 76% helix, 7% strand | Q7LC44 |
| B | Chains: B,D,F | protein | 6 | 0% helix, 67% strand | — |
| C | Activity-regulated cytoskeleton-associated protein | protein | 75 | 64% helix, 7% strand | Q7LC44 |
| D | Chains: B,D,F | protein | 7 | 0% helix, 57% strand | — |
| E | Activity-regulated cytoskeleton-associated protein | protein | 67 | 75% helix, 9% strand | Q7LC44 |
| F | Chains: B,D,F | protein | 8 | 0% helix, 63% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.48 | 0.80 | 21 | empty |
| 2 | 87 | 0.37 | 0.76 | 20 | empty |
Interfaces
6 interfaces between chains.
- E–F · 743 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 714 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 625 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 577 Ų buried · 6 hydrogen bonds · protein-protein
- A–E · 423 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6TNQ · Crystal structure of the human Arc N-lobe bound to repeat 4 from GKAP · the same entry in another collection · chain F against F, TM-score 1.00
- Q7LC44 · AlphaFold monomer V2.0 prediction for activity-regulated cytoskeleton-associated protein… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q7LC44
- Elsewhere: RCSB PDB 6TNQ · PDBe 6TNQ · UniProt Q7LC44
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.