Research workbench
Atomic resolution structure of achromobacter cycloclastes cu nitrite reductase with endogenously bound nitrite and no
Analyse Atomic resolution structure of achromobacter cycloclastes cu nitrite reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BWD
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper-containing nitrite reductase
- EC
- 1.7.2.1
- UniProt
- P25006
- Ligands
- HOA, CU, NO2
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper-containing nitrite reductase (EC 1.7.2.1) | protein | 334 | 11% helix, 40% strand | P25006 |
Ligands and binding sites
- HOA · Hydroxyamine · ligand · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- NO2 · Nitrite ion · ion · chains A
- ACT · Acetate ion · additive · 3 copies · chains A
- MLI · Malonate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.74 | 0.89 | 27 | empty |
Compared structures
- 2BWD · Atomic Resolution Structure of Achromobacter cycloclastes Cu Nitrite Reductase with… · the same entry in another collection · chain A against A, TM-score 1.00
- P25006 · AlphaFold monomer V2.0 prediction for copper-containing nitrite reductase (P25006) · a predicted model of the same protein · chain A 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 P25006
- Elsewhere: RCSB PDB 2BWD · PDBe 2BWD · UniProt P25006
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