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Crystal structure of endophilin-A1 bar domain
Analyse Crystal structure of endophilin-A1 bar domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZWW
- Type
- protein
- Length
- 395 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SH3-containing GRB2-like protein 2
- EC
- 2.3.1.-
- UniProt
- Q62420
- Ligands
- CD
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SH3-containing GRB2-like protein 2 (EC 2.3.1.-) | protein | 199 | 86% helix, 0% strand | Q62420 |
| B | SH3-containing GRB2-like protein 2 (EC 2.3.1.-) | protein | 196 | 86% helix, 0% strand | Q62420 |
Ligands and binding sites
- CD · Cadmium ion · metal · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 238 | 0.75 | 0.89 | 40 | empty |
| 2 | 94 | 0.44 | 0.79 | 19 | CD |
Interfaces
1 interface between chains.
- A–B · 2777 Ų buried · 19 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 Q62420
- Elsewhere: RCSB PDB 1ZWW · PDBe 1ZWW · UniProt Q62420
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