Research workbench
Crystal structure of the disulphide bond-deficient azurin mutant C3A/C26A: how important is the S-S bond for folding and stability?
Analyse Crystal structure of the disulphide bond-deficient azurin mutant C3A/C26A: how… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EZL
- Type
- protein
- Length
- 512 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Azurin
- UniProt
- P00282
- Ligands
- CU
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Azurin | protein | 128 | 17% helix, 34% strand | P00282 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 342 | 0.72 | 0.84 | 34 | empty |
| 2 | 198 | 0.71 | 0.89 | 34 | empty |
| 3 | 54 | 0.66 | 0.96 | 18 | empty |
| 4 | 231 | 0.61 | 0.81 | 41 | empty |
| 5 | 224 | 0.58 | 0.80 | 42 | empty |
Interfaces
6 interfaces between chains.
- A–C · 548 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 459 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 400 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 398 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 378 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1EZL · Crystal structure of the disulphide bond-deficient azurin mutant C3A/C26A: how important… · the same entry in another collection · chain D against D, TM-score 1.00
- P00282 · AlphaFold monomer V2.0 prediction for azurin (P00282) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P00282
- Elsewhere: RCSB PDB 1EZL · PDBe 1EZL · UniProt P00282
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