Research workbench
Crystal structure of a cyclase FAMC1 from fischerella ambigua utex 1903
Analyse Crystal structure of a cyclase FAMC1 from fischerella ambigua utex 1903 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YVK
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclase
- UniProt
- V5TER4
- Ligands
- 0HZ, CA
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclase | protein | 198 | 0% helix, 42% strand | V5TER4 |
Ligands and binding sites
- 0HZ · amino({3-[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]propyl}amino)methaniminium · ligand · chains A
- CA · Calcium ion · metal · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.79 | 0.93 | 26 | 0HZ |
Compared structures
- 5YVK · Crystal structure of a cyclase Famc1 from Fischerella ambigua UTEX 1903 · 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 V5TER4
- Elsewhere: RCSB PDB 5YVK · PDBe 5YVK · UniProt V5TER4
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