MolNFT v1 · #129185 · protein
A rare lysozyme crystal form solved using high-redundancy 3D electron diffraction data from micron-sized needle shaped crystals
5OCV: “A rare lysozyme crystal form solved using high-redundancy 3D electron diffraction data from micron-sized…”. Electron crystallography, 1 ligand (NA). MolNFT v1 #129185 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OCV
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- electron crystallography
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00698
- Ligands
- NA
Structure
electron crystallography · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 129 | — | P00698 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OCV · A Rare Lysozyme Crystal Form Solved Using High-Redundancy 3D Electron Diffraction Data… · 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 P00698
- Elsewhere: RCSB PDB 5OCV · PDBe 5OCV · UniProt P00698
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