Research workbench
Anti-HIV-1 Fab 2G12 in complex with glycopeptide 10V1S
Analyse Anti-HIV-1 Fab 2G12 in complex with glycopeptide 10V1S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CXG
- Type
- protein
- Length
- 899 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- MAN, BMA
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, K | — | protein | 213 | — | — |
| H | — | protein | 219 | — | — |
| M | — | protein | 224 | — | — |
| A | — | protein | 16 | — | — |
| C | — | protein | 14 | — | — |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 14 copies · chains A, L, H, K, M, C
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains L, H, A, K, M, C
- GOL · Glycerol · additive · 3 copies · chains L, M, H, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6CXG · anti-HIV-1 Fab 2G12 in complex with glycopeptide 10V1S · the same entry in another collection · chain L against L, 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
- Elsewhere: RCSB PDB 6CXG · PDBe 6CXG
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