Research workbench
Crystal structure of the double mutant CYS3SER/SER100PRO from pseudomonas aeruginosa at 1.8 a resolution
Analyse Crystal structure of the double mutant CYS3SER/SER100PRO from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GR7
- 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
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Azurin | protein | 127 | 20% helix, 35% strand | P00282 |
| B, C | Azurin | protein | 126 | 20% helix, 34% 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
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 | 223 | 0.65 | 0.84 | 37 | empty |
| 2 | 240 | 0.64 | 0.83 | 44 | empty |
| 3 | 189 | 0.63 | 0.84 | 38 | empty |
| 4 | 223 | 0.61 | 0.82 | 41 | empty |
Interfaces
6 interfaces between chains.
- A–D · 529 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 511 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 504 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 431 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 343 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation).
Compared structures
- 1GR7 · Crystal structure of the double mutant Cys3Ser/Ser100Pro from Pseudomonas Aeruginosa at… · 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 C 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 1GR7 · PDBe 1GR7 · UniProt P00282
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