MolNFT v2 · #127325 · protein
The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The sixth structure of the series with total exposition time 153 min.
5MHX: “The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum…”. X-ray diffraction at 1.35, 5 ligands (NAG, BMA, CU). MolNFT v2 #127325 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5MHX
- Type
- protein
- Length
- 499 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.35
- Source
- Steccherinum murashkinskyi
- UniProt
- I1VE66
- Ligands
- NAG, BMA, CU, NA, OXY
Structure
x-ray diffraction · resolution 1.35 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 499 | — | I1VE66 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies
- CU · Copper (II) ion · metal · 4 copies · chains A
- NA · Sodium ion · metal · chains A
- OXY · Oxygen molecule · ion · 2 copies · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5MHX · The study of the X-ray induced enzymatic reduction of molecular oxygen to water for… · 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 I1VE66
- Elsewhere: RCSB PDB 5MHX · PDBe 5MHX · UniProt I1VE66
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