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Crystal structure of flavocetin-a from the habu snake venom, a novel cyclic tetramer of C-type lectin-like heterodimers
Analyse Crystal structure of flavocetin-a from the habu snake venom, a novel cyclic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C3A
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavocetin-a: alpha subunit; Flavocetin-a: beta subunit
- UniProt
- Q8AV97, Q8AV98
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavocetin-a: alpha subunit | protein | 135 | 21% helix, 31% strand | Q8AV97 |
| B | Flavocetin-a: beta subunit | protein | 125 | 21% helix, 33% strand | Q8AV98 |
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 | 91 | 0.40 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1889 Ų buried · 39 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 1C3A · Crystal structure of flavocetin-a from the habu snake venom, a novel cyclic tetramer of… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8AV97 · AlphaFold monomer V2.0 prediction for snaclec flavocetin-a subunit alpha (Q8AV97) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q8AV98 · AlphaFold monomer V2.0 prediction for snaclec flavocetin-a subunit beta (Q8AV98) · a predicted model of the same protein · chain B 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 Q8AV97
- Every structure of UniProt Q8AV98
- Elsewhere: RCSB PDB 1C3A · PDBe 1C3A · UniProt Q8AV97 · UniProt Q8AV98
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