Research workbench
Fic protein from neisseria meningitidis (nmfic) mutant E102R in dimeric form
Analyse Fic protein from neisseria meningitidis (nmfic) mutant E102R in dimeric form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CGL
- Type
- protein
- Length
- 324 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine monophosphate-protein transferase nmfic
- EC
- 2.7.7.-
- UniProt
- Q7DDR9
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine monophosphate-protein transferase nmfic (EC 2.7.7.-) | protein | 161 | 65% helix, 3% strand | Q7DDR9 |
| B | Adenosine monophosphate-protein transferase nmfic (EC 2.7.7.-) | protein | 163 | 65% helix, 3% strand | Q7DDR9 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.67 | 0.91 | 26 | empty |
| 2 | 93 | 0.67 | 0.91 | 26 | empty |
| 3 | 249 | 0.50 | 0.75 | 44 | PEG |
Interfaces
1 interface between chains.
- A–B · 471 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5CGL · Fic protein from Neisseria meningitidis (NmFic) mutant E102R in dimeric form · the same entry in another collection · chain A against A, TM-score 1.00
- Q7DDR9 · AlphaFold monomer V2.0 prediction for protein adenylyltransferase nmfic (Q7DDR9) · a predicted model of the same protein · chain B 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 Q7DDR9
- Elsewhere: RCSB PDB 5CGL · PDBe 5CGL · UniProt Q7DDR9
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