Research workbench
X-ray crystal structure the two site-specific mutants ILE7SER and PHE110SER of azurin from pseudomonas aeruginosa
Analyse X-ray crystal structure the two site-specific mutants ILE7SER and PHE110SER of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ILS
- 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, NO3
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Azurin | protein | 128 | 16% helix, 34% strand | P00282 |
Ligands and binding sites
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 | 232 | 0.72 | 0.88 | 31 | empty |
| 2 | 308 | 0.68 | 0.83 | 38 | empty |
| 3 | 52 | 0.66 | 0.95 | 16 | empty |
| 4 | 201 | 0.59 | 0.81 | 42 | empty |
| 5 | 271 | 0.59 | 0.79 | 41 | empty |
Interfaces
6 interfaces between chains.
- A–C · 532 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 519 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 432 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 409 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 396 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1ILS · X-ray crystal structure the two site-specific mutants ILE7SER and PHE110SER of azurin… · 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 0.99
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 1ILS · PDBe 1ILS · UniProt P00282
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