Research workbench
Crystal structure of the inhibited form of the redox-sensitive sufe- like sulfur acceptor csde from escherichia COLI at 2.40 ångström resolution
Analyse Crystal structure of the inhibited form of the redox-sensitive sufe- like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NQ6
- Type
- protein
- Length
- 283 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfur acceptor protein csde
- UniProt
- P0AGF2
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfur acceptor protein csde | protein | 141 | 48% helix, 16% strand | P0AGF2 |
| B | Sulfur acceptor protein csde | protein | 142 | 49% helix, 16% strand | P0AGF2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 223 | 0.56 | 0.79 | 31 | GOL |
| 2 | 68 | 0.33 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 445 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5NQ6 · Crystal structure of the inhibited form of the redox-sensitive SufE-like sulfur acceptor… · the same entry in another collection · chain A against A, TM-score 1.00
- P0AGF2 · AlphaFold monomer V2.0 prediction for sulfur acceptor protein csde (P0AGF2) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P0AGF2
- Elsewhere: RCSB PDB 5NQ6 · PDBe 5NQ6 · UniProt P0AGF2
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