Research workbench
Acetyltransferase domain of pglb from neisseria gonorrhoeae FA1090
Analyse Acetyltransferase domain of pglb from neisseria gonorrhoeae FA1090 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M98
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pilin glycosylation protein
- UniProt
- Q5FAE1
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pilin glycosylation protein | protein | 205 | 15% helix, 30% strand | Q5FAE1 |
Compared structures
- 4M98 · Acetyltransferase domain of PglB from Neisseria gonorrhoeae FA1090 · 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 4M98 · PDBe 4M98 · UniProt Q5FAE1
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