Research workbench
X-ray crystal structure of pseudoazurin MET16GLY variant
Analyse X-ray crystal structure of pseudoazurin MET16GLY variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WV4
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pseudoazurin
- UniProt
- P19567
- Ligands
- CU
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pseudoazurin | protein | 124 | 15% helix, 35% strand | P19567 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 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 | 229 | 0.65 | 0.83 | 39 | empty |
| 2 | 77 | 0.35 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 385 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- P19567 · AlphaFold monomer V2.0 prediction for pseudoazurin (P19567) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P19567
- Elsewhere: RCSB PDB 5WV4 · PDBe 5WV4 · UniProt P19567
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