Research workbench
Crystal structure of the azurin mutant PHE114ALA from pseudomonas aeruginosa at 2.6 ångströms resolution
Analyse Crystal structure of the azurin mutant PHE114ALA from pseudomonas aeruginosa at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AZN
- 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
- 9 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Azurin | protein | 128 | 17% helix, 28% 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
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.60 | 0.81 | 38 | empty |
| 2 | 341 | 0.56 | 0.76 | 36 | empty |
| 3 | 135 | 0.45 | 0.77 | 21 | empty |
| 4 | 126 | 0.45 | 0.77 | 19 | empty |
| 5 | 104 | 0.40 | 0.77 | 21 | empty |
Interfaces
4 interfaces between chains.
- A–C · 456 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 399 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 396 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 121 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1AZN · Crystal structure of the azurin mutant PHE114ALA from pseudomonas aeruginosa at 2.6… · the same entry in another collection · chain A against A, TM-score 1.00
- P00282 · AlphaFold monomer V2.0 prediction for azurin (P00282) · a predicted model of the same protein · chain A 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 1AZN · PDBe 1AZN · UniProt P00282
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