MolNFT v1 · #13727 · protein
Hevamine a (a plant ENDOCHITINASE/LYSOZYME) complexed with allosamidin
1LLO · Hevamine-a: “Hevamine a (a plant ENDOCHITINASE/LYSOZYME) complexed with allosamidin”. X-ray diffraction, 2 ligands (AMI, NAA), 1 pocket (best druggability 0.41). MolNFT v1 #13727 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1LLO
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hevamine-a
- EC
- 3.2.1.14, 3.2.1.17
- UniProt
- P23472
- Ligands
- AMI, NAA
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hevamine-a (EC 3.2.1.14, 3.2.1.17) | protein | 273 | 38% helix, 20% strand | P23472 |
Ligands and binding sites
- AMI · Allosamizoline · ligand · chains A
- NAA · 2-acetamido-2-deoxy-beta-D-allopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.41 | 0.77 | 28 | NAA, AMI |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 P23472
- Elsewhere: RCSB PDB 1LLO · PDBe 1LLO · UniProt P23472
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