Research workbench
Pseudomonas aeruginosa azurin with mutated metal-binding loop sequence (caaaahaaam)
Analyse Pseudomonas aeruginosa azurin with mutated metal-binding loop sequence… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FSW
- Type
- protein
- Length
- 506 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Azurin
- UniProt
- P00282
- Ligands
- CU
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Azurin | protein | 127 | 21% helix, 34% strand | P00282 |
| B | Azurin | protein | 128 | 16% helix, 34% strand | P00282 |
| C | Azurin | protein | 124 | 15% helix, 35% 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
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 | 973 | 0.72 | 0.76 | 71 | empty |
| 2 | 61 | 0.31 | 0.75 | 15 | empty |
Interfaces
5 interfaces between chains.
- A–C · 762 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 447 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 407 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 206 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 24 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3FSW · Pseudomonas aeruginosa Azurin with mutated metal-binding loop sequence (CAAAAHAAAM) · the same entry in another collection · chain C against C, 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 0.99
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 3FSW · PDBe 3FSW · UniProt P00282
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