Research workbench
Crystal structure of mutant (M182T)OF nitrite reductase
Analyse Crystal structure of mutant (M182T)OF nitrite reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MZZ
- Type
- protein
- Length
- 1,002 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper-containing nitrite reductase
- EC
- 1.7.99.3
- UniProt
- Q53239
- Ligands
- CU
- Pockets
- 12 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Copper-containing nitrite reductase (EC 1.7.99.3) | protein | 334 | 11% helix, 43% strand | Q53239 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.85 | 0.97 | 30 | empty |
| 2 | 353 | 0.73 | 0.85 | 44 | empty |
| 3 | 130 | 0.47 | 0.78 | 29 | empty |
| 4 | 107 | 0.46 | 0.79 | 23 | empty |
| 5 | 141 | 0.45 | 0.76 | 26 | empty |
Interfaces
3 interfaces between chains.
- A–C · 2306 Ų buried · 42 hydrogen bonds · protein-protein
- B–C · 2293 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 2285 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 1MZZ · Crystal Structure of Mutant (M182T)of Nitrite Reductase · the same entry in another collection · chain A against A, TM-score 1.00
- Q53239 · AlphaFold monomer V2.0 prediction for copper-containing nitrite reductase (Q53239) · a predicted model of the same protein · 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 Q53239
- Elsewhere: RCSB PDB 1MZZ · PDBe 1MZZ · UniProt Q53239
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