MolNFT v1 · #99632 · protein
Acetyltransferase domain of pglb from neisseria gonorrhoeae FA1090 in complex with acetyl coenzyme a
4M99 · Pilin glycosylation protein: “Acetyltransferase domain of pglb from neisseria gonorrhoeae FA1090 in complex with acetyl coenzyme a”. X-ray diffraction, 2 ligands (ACO, NA), 4 pockets (best druggability 0.71). MolNFT v1 #99632 on…
- PDB
- 4M99
- Type
- protein
- Length
- 617 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pilin glycosylation protein
- UniProt
- Q5FAE1
- Ligands
- ACO, NA
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Pilin glycosylation protein | protein | 206 | 15% helix, 31% strand | Q5FAE1 |
| B | Pilin glycosylation protein | protein | 205 | 14% helix, 31% strand | Q5FAE1 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 3 copies · chains A, B, C
- NA · Sodium ion · metal · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.71 | 0.99 | 27 | empty |
| 2 | 217 | 0.55 | 0.78 | 37 | ACO |
| 3 | 240 | 0.54 | 0.77 | 42 | ACO |
| 4 | 161 | 0.51 | 0.79 | 39 | ACO |
Interfaces
3 interfaces between chains.
- A–C · 831 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 818 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 817 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4M99 · Acetyltransferase domain of PglB from Neisseria gonorrhoeae FA1090 in complex with acetyl… · the same entry in another collection · chain A 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 Q5FAE1
- Elsewhere: RCSB PDB 4M99 · PDBe 4M99 · UniProt Q5FAE1
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