MolNFT v1 · #123416 · protein
Fic-1 (AA134 - 508) from C. elegans
5JJ6 · Adenosine monophosphate-protein transferase ficd homolog: “Fic-1 (AA134 - 508) from C. elegans”. X-ray diffraction, 1 ligand (SO4), 11 pockets (best druggability 0.44). MolNFT v1 #123416 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5JJ6
- Type
- protein
- Length
- 663 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine monophosphate-protein transferase ficd homolog
- EC
- 2.7.7.-
- UniProt
- Q23544
- Ligands
- SO4
- Pockets
- 11 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine monophosphate-protein transferase ficd homolog (EC 2.7.7.-) | protein | 330 | 70% helix, 0% strand | Q23544 |
| B | Adenosine monophosphate-protein transferase ficd homolog (EC 2.7.7.-) | protein | 333 | 69% helix, 1% strand | Q23544 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.44 | 0.77 | 16 | empty |
| 2 | 73 | 0.44 | 0.81 | 12 | empty |
| 3 | 168 | 0.41 | 0.73 | 30 | empty |
| 4 | 149 | 0.40 | 0.73 | 24 | empty |
| 5 | 111 | 0.38 | 0.75 | 21 | SO4 |
Interfaces
1 interface between chains.
- A–B · 690 Ų buried · 12 hydrogen bonds · protein-protein
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 Q23544
- Elsewhere: RCSB PDB 5JJ6 · PDBe 5JJ6 · UniProt Q23544
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