MolNFT v1 · #78526 · protein
RUSSELL'S viper venom serine proteinase, rvv-V (ppack-bound form)
3SBK · Vipera russelli proteinase rvv-V gamma: “RUSSELL'S viper venom serine proteinase, rvv-V (ppack-bound form)”. X-ray diffraction, 2 ligands (0G6, NAG), 1 pocket (best druggability 0.54). MolNFT v1 #78526 on GenesisL1: 3D structure…
- PDB
- 3SBK
- Type
- protein
- Length
- 234 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vipera russelli proteinase rvv-V gamma
- EC
- 3.4.21.95
- UniProt
- P18965
- Ligands
- 0G6, NAG
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vipera russelli proteinase rvv-V gamma (EC 3.4.21.95) | protein | 234 | 11% helix, 35% strand | P18965 |
Ligands and binding sites
- 0G6 · D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide · ligand · chains A
- 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.54 | 0.80 | 33 | 0G6 |
Modifications
Observed in the structure: 6 disulfide, 2 covalent, 1 glycan (disulfide, covalent ligand, N-glycosylation).
Compared structures
- 3SBK · Russell's viper venom serine proteinase, RVV-V (PPACK-bound form) · the same entry in another collection · chain A against A, TM-score 1.00
- P18965 · AlphaFold monomer V2.0 prediction for factor V activator rvv-V gamma (P18965) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P18965
- Elsewhere: RCSB PDB 3SBK · PDBe 3SBK · UniProt P18965
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