Research workbench
Cryo-EM structure of the VRC316 clinical trial, vaccine-elicited, human antibody 316-310-1B11 in complex with an H2 CAN05 ha trimer
Analyse Cryo-EM structure of the VRC316 clinical trial, vaccine-elicited, human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L0L
- Type
- protein
- Length
- 2,166 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4ZH98
- Ligands
- NAG
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, J, K | — | protein | 108 | — | — |
| A, C, D | — | protein | 322 | — | Q4ZH98 |
| B, E, F | — | protein | 172 | — | Q4ZH98 |
| H, G, I | — | protein | 120 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 15 copies · chains A, B, C, E, D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7L0L · Cryo-EM structure of the VRC316 clinical trial, vaccine-elicited, human antibody… · 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
- Every structure of UniProt Q4ZH98
- Elsewhere: RCSB PDB 7L0L · PDBe 7L0L · UniProt Q4ZH98
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