Research workbench
Structure of M92A variant of three-domain heme-cu nitrite reductase from ralstonia pickettii
Analyse Structure of M92A variant of three-domain heme-cu nitrite reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZBM
- Type
- protein
- Length
- 455 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
- E2STD2
- Ligands
- HEC, CU
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper-containing nitrite reductase (EC 1.7.2.1) | protein | 455 | 21% helix, 33% strand | E2STD2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.76 | 0.90 | 35 | HEC |
| 2 | 284 | 0.58 | 0.77 | 34 | empty |
| 3 | 167 | 0.45 | 0.75 | 29 | empty |
| 4 | 69 | 0.43 | 0.81 | 21 | empty |
| 5 | 109 | 0.42 | 0.77 | 24 | empty |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 3ZBM · Structure of M92A variant of three-domain heme-Cu nitrite reductase from Ralstonia… · 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 E2STD2
- Elsewhere: RCSB PDB 3ZBM · PDBe 3ZBM · UniProt E2STD2
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