Research workbench
Azurin H117G, oxidized form
Analyse Azurin H117G, oxidized form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N2J
- Type
- protein
- Length
- 1,536 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Azurin
- UniProt
- P00282
- Ligands
- CU
- Pockets
- 15 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Azurin | protein | 128 | 15% helix, 34% strand | P00282 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 24 copies · chains A, D, B, C, E, G, F, H, I, J, L, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 978 | 0.83 | 0.84 | 124 | empty |
| 2 | 699 | 0.79 | 0.84 | 97 | empty |
| 3 | 955 | 0.76 | 0.79 | 120 | empty |
| 4 | 144 | 0.66 | 0.88 | 27 | CU |
| 5 | 247 | 0.65 | 0.83 | 39 | CU |
Interfaces
26 interfaces between chains.
- E–G · 375 Ų buried · 3 hydrogen bonds · protein-protein
- E–I · 374 Ų buried · 1 hydrogen bond · protein-protein
- C–F · 351 Ų buried · 5 hydrogen bonds · protein-protein
- J–L · 350 Ų buried · 2 hydrogen bonds · protein-protein
- H–J · 350 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 3N2J · Azurin H117G, oxidized form · the same entry in another collection · chain L against L, TM-score 1.00
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 3N2J · PDBe 3N2J · UniProt P00282
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