Research workbench
Structure of oxidized C73S putidaredoxin from pseudomonas putida
Analyse Structure of oxidized C73S putidaredoxin from pseudomonas putida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XLP
- Type
- protein
- Length
- 318 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putidaredoxin
- EC
- 1.9.3.2
- UniProt
- P00259
- Ligands
- FES
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Putidaredoxin (EC 1.9.3.2) | protein | 106 | 18% helix, 22% strand | P00259 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 3 copies · chains A, B, C
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 | 107 | 0.44 | 0.78 | 18 | empty |
| 2 | 58 | 0.29 | 0.75 | 18 | empty |
Interfaces
2 interfaces between chains.
- A–C · 507 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 191 Ų buried · 1 hydrogen bond · protein-protein
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 P00259
- Elsewhere: RCSB PDB 1XLP · PDBe 1XLP · UniProt P00259
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