MolNFT v1 · #31588 · protein
X-ray crystal structure of the two site-specific mutants HIS35*GLN and HIS35*LEU of azurin from pseudomonas aeruginosa
2AZU: “X-ray crystal structure of the two site-specific mutants HIS35*GLN and HIS35*LEU of azurin from pseudomonas…”. X-ray diffraction, 2 ligands (CU, NO3), 4 pockets (best druggability 0.73). MolNFT v1 #31588 on GenesisL1: 3D structure…
- PDB
- 2AZU
- 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
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Azurin | protein | 128 | 19% helix, 34% strand | P00282 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.73 | 0.87 | 34 | empty |
| 2 | 266 | 0.65 | 0.82 | 41 | empty |
| 3 | 310 | 0.63 | 0.80 | 47 | empty |
| 4 | 253 | 0.61 | 0.80 | 44 | empty |
Interfaces
6 interfaces between chains.
- A–C · 544 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 517 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 407 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 407 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 391 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2AZU · X-ray crystal structure of the two site-specific mutants HIS35*GLN and HIS35*LEU of… · 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 2AZU · PDBe 2AZU · UniProt P00282
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