Research workbench
Crystal structure of RE(PHEN)(CO)3 (THR124HIS)(HIS83GLN) azurin CU(II) from pseudomonas aeruginosa
Analyse Crystal structure of RE(PHEN)(CO)3 (THR124HIS)(HIS83GLN) azurin CU(II) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I7S
- Type
- protein
- Length
- 512 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Azurin
- UniProt
- P00282
- Ligands
- REP, CON, CU
- Pockets
- 3 · best druggability 0.52
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
- REP · (1,10 phenanthroline)-(tri-carbon monoxide) rhenium (I) · ligand · 4 copies · chains A, B, C, D
- CON · Cobalt tetraammine ion · ligand · chains B
- 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
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 161 | 0.52 | 0.79 | 31 | empty |
| 2 | 95 | 0.47 | 0.80 | 19 | empty |
| 3 | 97 | 0.33 | 0.72 | 16 | empty |
Interfaces
4 interfaces between chains.
- B–D · 500 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 490 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 58 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 25 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2I7S · Crystal structure of Re(phen)(CO)3 (Thr124His)(His83Gln) Azurin Cu(II) from Pseudomonas… · 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 D 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 2I7S · PDBe 2I7S · UniProt P00282
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