Research workbench
Fic protein from Neisseria meningitidis mutant E186G in complex with AMPPNP
Analyse Fic protein from Neisseria meningitidis mutant E186G in complex with AMPPNP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZLM
- Type
- protein
- Length
- 177 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- NEISSERIA MENINGITIDIS
- Molecule
- Adenosine monophosphate-protein transferase nmfic
- EC
- 2.7.7.-
- UniProt
- Q7DDR9
- Ligands
- ANP, MG
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 60% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine monophosphate-protein transferase nmfic (EC 2.7.7.-) | protein | 177 | 60% helix, 5% strand | Q7DDR9 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.67 | 0.91 | 25 | empty |
| 2 | 236 | 0.55 | 0.77 | 27 | ANP, MG |
Compared structures
- 3ZLM · Fic protein from neisseria meningitidis mutant E186G in complex with amppnp · 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 A 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 Q7DDR9
- Elsewhere: RCSB PDB 3ZLM · PDBe 3ZLM · UniProt Q7DDR9
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