Research workbench
Cryo-EM structure of CH235UCA bound to MAN5-enriched CH505.N279K.G458Y.SOSIP.664
Analyse Cryo-EM structure of CH235UCA bound to MAN5-enriched CH505.N279K.G458Y.SOSIP.664 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UDA
- Type
- protein
- Length
- 3,024 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- M4M0W3, Q2N0S5
- Ligands
- NAG, BMA, MAN
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, I | — | protein | 452 | — | M4M0W3 |
| C, G, K | — | protein | 220 | — | — |
| Z, F, J | — | protein | 126 | — | Q2N0S5 |
| D, H, L | — | protein | 210 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, E, I
- BMA · beta-D-mannopyranose · sugar · 3 copies
- MAN · alpha-D-mannopyranose · sugar · 3 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UDA · Cryo-EM structure of CH235UCA bound to Man5-enriched CH505.N279K.G458Y.SOSIP.664 · 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 M4M0W3
- Every structure of UniProt Q2N0S5
- Elsewhere: RCSB PDB 6UDA · PDBe 6UDA · UniProt M4M0W3 · UniProt Q2N0S5
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