Research workbench
Vexl: a periplasmic depolymerase provides new insight into ABC transporter-dependent secretion of bacterial capsular polysaccharides
Analyse Vexl: a periplasmic depolymerase provides new insight into ABC… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FI2
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vexl
- UniProt
- A0A160EBC2
- Ligands
- DJB, DJE
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vexl | protein | 375 | 13% helix, 34% strand | A0A160EBC2 |
Ligands and binding sites
- DJB · 3-O-acetyl-2-acetamido-2-deoxy-alpha-D-galactopyranuronic acid · ligand · 2 copies · chains A
- DJE · 2-acetamido-2-deoxy-alpha-D-galactopyranuronic acid · ligand · chains A
- MLI · Malonate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6FI2 · VexL: A periplasmic depolymerase provides new insight into ABC transporter-dependent… · 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 A0A160EBC2
- Elsewhere: RCSB PDB 6FI2 · PDBe 6FI2 · UniProt A0A160EBC2
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