MolNFT v1 · #126936 · protein
The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from steccherinum MURASHKINSKYI.THE fourth structure of the series with total exposition time 93 min.
5MHV: “The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from steccherinum…”. X-ray diffraction, 5 ligands (NAG, BMA, CU). MolNFT v1 #126936 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5MHV
- Type
- protein
- Length
- 499 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- I1VE66
- Ligands
- NAG, BMA, CU, NA, OXY
Structure
x-ray diffraction · 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
- 5MHV · 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 5MHV · PDBe 5MHV · UniProt I1VE66
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