Research workbench
Fic protein from neisseria meningitidis (nmfic) mutant E156R Y183F in dimeric form
Analyse Fic protein from neisseria meningitidis (nmfic) mutant E156R Y183F in dimeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CMT
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine monophosphate-protein transferase nmfic
- EC
- 2.7.7.-
- UniProt
- Q7DDR9
- Ligands
- CL
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine monophosphate-protein transferase nmfic (EC 2.7.7.-) | protein | 180 | 60% helix, 4% strand | Q7DDR9 |
Ligands and binding sites
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 | 71 | 0.72 | 0.96 | 19 | empty |
| 2 | 234 | 0.57 | 0.78 | 25 | GOL, CL |
Compared structures
- 5CMT · Fic protein from Neisseria meningitidis (NmFic) mutant E156R Y183F 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 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 5CMT · PDBe 5CMT · UniProt Q7DDR9
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