MolNFT v1 · #10774 · protein
Structure of pokeweed antiviral protein from seeds (pap-S1)
1J1Q · Antiviral protein S: “Structure of pokeweed antiviral protein from seeds (pap-S1)”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.49). MolNFT v1 #10774 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1J1Q
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antiviral protein S
- EC
- 3.2.2.22
- UniProt
- P23339
- Ligands
- NAG
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antiviral protein S (EC 3.2.2.22) | protein | 261 | 39% helix, 23% strand | P23339 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 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 | 130 | 0.49 | 0.79 | 23 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
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 P23339
- Elsewhere: RCSB PDB 1J1Q · PDBe 1J1Q · UniProt P23339
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