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Structure of alcaligenes xylosoxidans nitrite reductase in space group R3 - 2 of 2
Analyse Structure of alcaligenes xylosoxidans nitrite reductase in space group R3 - 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VM4
- Type
- protein
- Length
- 334 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, ZN
- Pockets
- 1 · best druggability 0.40
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 | 334 | 11% helix, 39% strand | O68601 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
- PG4 · Tetraethylene glycol · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.40 | 0.78 | 17 | empty |
Compared structures
- 2VM4 · Structure of Alcaligenes xylosoxidans nitrite reductase in space group R3 - 2 of 2 · 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 2VM4 · PDBe 2VM4 · UniProt O68601
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