Research workbench
Crystal structure of 438-B11 Fab in complex with an uncleaved prefusion optimized (ufo) soluble BG505 trimer and Fab 35O22 at 3.80 ångström
Analyse Crystal structure of 438-B11 Fab in complex with an uncleaved prefusion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UTK
- Type
- protein
- Length
- 1,484 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2N0S6, Q2N0S9
- Ligands
- NAG, MAN, BMA
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | — | protein | 240 | — | — |
| E | — | protein | 213 | — | — |
| L | — | protein | 213 | — | — |
| G | — | protein | 453 | — | Q2N0S6 |
| T | — | protein | 134 | — | Q2N0S9 |
| H | — | protein | 231 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 40 copies · chains L, G, H, D, T, E
- MAN · alpha-D-mannopyranose · sugar · 26 copies · chains H, L, D, E, G
- BMA · beta-D-mannopyranose · sugar · 12 copies · chains H, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UTK · Crystal structure of 438-B11 Fab in complex with an uncleaved prefusion optimized (UFO)… · the same entry in another collection · chain D against D, 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 Q2N0S6
- Every structure of UniProt Q2N0S9
- Elsewhere: RCSB PDB 6UTK · PDBe 6UTK · UniProt Q2N0S6 · UniProt Q2N0S9
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