Research workbench
Fic protein from neisseria meningitidis mutant S182A/E186A in complex with amppnp
Analyse Fic protein from neisseria meningitidis mutant S182A/E186A in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SN9
- Type
- protein
- Length
- 2,528 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell filamentation protein fic-related protein
- UniProt
- Q7DDR9
- Ligands
- ANP
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Cell filamentation protein fic-related protein | protein | 158 | 59% helix, 6% strand | Q7DDR9 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.84 | 0.85 | 110 | ANP |
| 2 | 1081 | 0.83 | 0.84 | 98 | ANP |
| 3 | 1023 | 0.76 | 0.79 | 88 | ANP |
| 4 | 458 | 0.72 | 0.82 | 52 | empty |
| 5 | 631 | 0.69 | 0.77 | 43 | empty |
Interfaces
32 interfaces between chains.
- I–O · 831 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 827 Ų buried · 13 hydrogen bonds · protein-protein
- C–E · 826 Ų buried · 13 hydrogen bonds · protein-protein
- G–L · 824 Ų buried · 12 hydrogen bonds · protein-protein
- K–P · 818 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3SN9 · Fic protein from NEISSERIA MENINGITIDIS mutant S182A/E186A in complex with AMPPNP · the same entry in another collection · chain P against P, 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 Q7DDR9
- Elsewhere: RCSB PDB 3SN9 · PDBe 3SN9 · UniProt Q7DDR9
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