MolNFT v1 · #187889 · protein
Crystal structure of the anti-CD4 adnectin 6940_B01 as a complex with the extracellular domains of CD4 and ibalizumab Fab
7T0R: “Crystal structure of the anti-CD4 adnectin 6940_B01 as a complex with the extracellular domains of CD4 and…”. X-ray diffraction, 2 ligands (NAG, SO4). MolNFT v1 #187889 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7T0R
- Type
- protein
- Length
- 1,773 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01730
- Ligands
- NAG, SO4
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 216 | — | — |
| H | — | protein | 221 | — | — |
| A | — | protein | 355 | — | P01730 |
| B | — | protein | 215 | — | — |
| C | — | protein | 222 | — | — |
| D | — | protein | 357 | — | P01730 |
| G | — | protein | 93 | — | — |
| I | — | protein | 94 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, D
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7T0R · Crystal structure of the anti-CD4 adnectin 6940_B01 as a complex with the extracellular… · the same entry in another collection · chain I against I, TM-score 1.00
- P01730 · AlphaFold monomer V2.0 prediction for T-cell surface glycoprotein CD4 (P01730) · a predicted model of the same protein · chain A against A, TM-score 0.55
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 P01730
- Elsewhere: RCSB PDB 7T0R · PDBe 7T0R · UniProt P01730
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.