Research workbench
Superoxide reductase (neelaredoxin) from archaeoglobus fulgidus E12Q mutant in the reduced form
Analyse Superoxide reductase (neelaredoxin) from archaeoglobus fulgidus E12Q mutant in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C4U
- Type
- protein
- Length
- 1,968 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide reductase
- EC
- 1.15.1.2
- UniProt
- O29903
- Ligands
- FE2
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Superoxide reductase (EC 1.15.1.2) | protein | 123 | 0% helix, 54% strand | O29903 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.85 | 0.97 | 43 | empty |
| 2 | 245 | 0.85 | 0.97 | 43 | empty |
| 3 | 243 | 0.85 | 0.97 | 41 | empty |
| 4 | 246 | 0.84 | 0.96 | 43 | empty |
| 5 | 229 | 0.84 | 0.97 | 42 | empty |
Interfaces
32 interfaces between chains.
- K–L · 1240 Ų buried · 21 hydrogen bonds · protein-protein
- M–N · 1230 Ų buried · 21 hydrogen bonds · protein-protein
- G–H · 1221 Ų buried · 17 hydrogen bonds · protein-protein
- I–J · 1213 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1200 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4C4U · Superoxide reductase (Neelaredoxin) from Archaeoglobus fulgidus E12Q mutant in the… · the same entry in another collection · chain P against P, 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 O29903
- Elsewhere: RCSB PDB 4C4U · PDBe 4C4U · UniProt O29903
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