Research workbench
C-terminal domain of harc in complex with nanobodies H11 and C11, collapsed crystal form
Analyse C-terminal domain of harc in complex with nanobodies H11 and C11, collapsed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R1Z
- Type
- protein
- Length
- 362 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nbarc-H11; Activity-regulated cytoskeleton-associated protein; Nbarc-C11
- UniProt
- Q7LC44
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Nbarc-H11 | protein | 125 | 12% helix, 47% strand | — |
| A | Activity-regulated cytoskeleton-associated protein | protein | 119 | 71% helix, 2% strand | Q7LC44 |
| C | Nbarc-C11 | protein | 118 | 3% helix, 52% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.66 | 0.83 | 34 | empty |
| 2 | 56 | 0.35 | 0.78 | 16 | empty |
Interfaces
2 interfaces between chains.
- E–A · 1181 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 676 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7R1Z · C-terminal domain of hArc in complex with nanobodies H11 and C11, collapsed crystal form · the same entry in another collection · chain E against E, 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 0.53
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 7R1Z · PDBe 7R1Z · UniProt Q7LC44
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