Research workbench
Crystal structure of DPR10 IG1 bound to dip-alpha IG1
Analyse Crystal structure of DPR10 IG1 bound to dip-alpha IG1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NRQ
- Type
- protein
- Length
- 426 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9VT83, Q9W4R3
- Ligands
- NAG, FUC, BMA, MAN
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 109 | — | Q9VT83 |
| B | — | protein | 104 | — | Q9W4R3 |
| C | — | protein | 108 | — | Q9VT83 |
| D | — | protein | 105 | — | Q9W4R3 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, C, B, D
- FUC · alpha-L-fucopyranose · sugar · 8 copies · chains A, B, D, C
- BMA · beta-D-mannopyranose · sugar · 2 copies
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains B
- GOL · Glycerol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6NRQ · Crystal structure of Dpr10 IG1 bound to DIP-alpha IG1 · 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 Q9VT83
- Every structure of UniProt Q9W4R3
- Elsewhere: RCSB PDB 6NRQ · PDBe 6NRQ · UniProt Q9VT83 · UniProt Q9W4R3
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