Research workbench
Crystal structure of P24BETA1 gold domain
Analyse Crystal structure of P24BETA1 gold domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AZW
- Type
- protein
- Length
- 187 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane EMP24 domain-containing protein 2
- UniProt
- Q15363
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane EMP24 domain-containing protein 2 | protein | 94 | 0% helix, 64% strand | Q15363 |
| B | Transmembrane EMP24 domain-containing protein 2 | protein | 93 | 0% helix, 67% strand | Q15363 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.54 | 0.80 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 331 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q15363
- Elsewhere: RCSB PDB 5AZW · PDBe 5AZW · UniProt Q15363
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