Research workbench
E. COLI F17A-G lectin domain complex with GLCNAC(BETA1-O)ME
Analyse E. COLI F17A-G lectin domain complex with GLCNAC(BETA1-O)ME in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZPL
- Type
- protein
- Length
- 336 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F17A-G
- UniProt
- Q99003
- Ligands
- MAG
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | F17A-G | protein | 168 | 2% helix, 59% strand | Q99003 |
Ligands and binding sites
- MAG · methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.51 | 0.74 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 313 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q99003
- Elsewhere: RCSB PDB 1ZPL · PDBe 1ZPL · UniProt Q99003
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