MolNFT v1 · #181415 · protein
Cryo-EM structure of DH851.3 bound to HIV-1 CH505 env
7LU9: “Cryo-EM structure of DH851.3 bound to HIV-1 CH505 env”. Electron microscopy, 3 ligands (NAG, BMA, MAN). MolNFT v1 #181415 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LU9
- Type
- protein
- Length
- 4,383 residues
- Chains
- 18
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- M4M097
- Ligands
- NAG, BMA, MAN
Structure
electron microscopy · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| k, j, r | — | protein | 209 | — | — |
| l, i, q | — | protein | 228 | — | — |
| m, h, p | — | protein | 222 | — | — |
| n, g, o | — | protein | 206 | — | — |
| a, b, c | — | protein | 135 | — | — |
| d, e, f | — | protein | 461 | — | M4M097 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 51 copies · chains a, d, h, b, e, l, c, f, q
- BMA · beta-D-mannopyranose · sugar · 18 copies · chains d, e, p
- MAN · alpha-D-mannopyranose · sugar · 18 copies · chains i, g, h, d, m, l, e, p, q, r, f
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LU9 · Cryo-EM structure of DH851.3 bound to HIV-1 CH505 Env · the same entry in another collection · chain k against k, 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 M4M097
- Elsewhere: RCSB PDB 7LU9 · PDBe 7LU9 · UniProt M4M097
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