Research workbench
Atomic resolution structure of D92E mutant of alcaligenes xylosoxidans nitrite reductase
Analyse Atomic resolution structure of D92E mutant of alcaligenes xylosoxidans nitrite… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OE2
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dissimilatory copper-containing nitrite reductase
- UniProt
- O68601
- Ligands
- CU
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dissimilatory copper-containing nitrite reductase | protein | 335 | 11% helix, 39% strand | O68601 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.39 | 0.78 | 17 | empty |
Modifications
Observed in the structure: 1 modified (cyclization).
Compared structures
- 1OE2 · Atomic Resolution Structure of D92E Mutant of Alcaligenes xylosoxidans Nitrite Reductase · the same entry in another collection · chain A against A, 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 O68601
- Elsewhere: RCSB PDB 1OE2 · PDBe 1OE2 · UniProt O68601
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