Research workbench
Crystal structure of the fimh-binding decoy module of human glycoprotein 2 (GP2) (crystal form III)
Analyse Crystal structure of the fimh-binding decoy module of human glycoprotein 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P6T
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform alpha of pancreatic secretory granule membrane major glycoprotein GP2
- UniProt
- P55259
- Ligands
- 9D2, NAG
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform alpha of pancreatic secretory granule membrane major glycoprotein GP2 | protein | 138 | 4% helix, 34% strand | P55259 |
Ligands and binding sites
- 9D2 · 2-ethyl-2-(hydroxymethyl)propane-1,3-diol · ligand · 5 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 7P6T · Crystal structure of the FimH-binding decoy module of human glycoprotein 2 (GP2) (crystal… · the same entry in another collection · chain A against A, TM-score 1.00
- P55259 · AlphaFold monomer V2.0 prediction for pancreatic secretory granule membrane major… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P55259
- Elsewhere: RCSB PDB 7P6T · PDBe 7P6T · UniProt P55259
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