Research workbench
Pseudomonas aeruginosa E2Q/H83Q/M109H-azurin RE(PHEN)(CO)3
Analyse Pseudomonas aeruginosa E2Q/H83Q/M109H-azurin RE(PHEN)(CO)3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FNW
- Type
- protein
- Length
- 256 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Azurin
- UniProt
- P00282
- Ligands
- REP, CU
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Azurin | protein | 128 | 21% helix, 35% strand | P00282 |
Ligands and binding sites
- REP · (1,10 phenanthroline)-(tri-carbon monoxide) rhenium (I) · ligand · 2 copies · chains A, B
- CU · Copper (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.33 | 0.75 | 15 | empty |
| 2 | 58 | 0.27 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 463 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 2FNW · PDBe 2FNW · UniProt P00282
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