MolNFT v1 · #180628 · protein
C-type carbohydrate-recognition domain 4 of the mannose receptor complexed with L-fucose-(alpha 1-2)-D-galactose-(BETA1-4)-D-glucose
7L61 · Macrophage mannose receptor 1: “C-type carbohydrate-recognition domain 4 of the mannose receptor complexed with L-fucose-(alpha…”. X-ray diffraction, 4 ligands (BGC, GAL, FUC). MolNFT v1 #180628 on GenesisL1: 3D structure, binding…
- PDB
- 7L61
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrophage mannose receptor 1
- UniProt
- P22897
- Ligands
- BGC, GAL, FUC, CA
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage mannose receptor 1 | protein | 122 | 25% helix, 28% strand | P22897 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · chains A
- GAL · beta-D-galactopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7L61 · C-type carbohydrate-recognition domain 4 of the mannose receptor complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P22897 · AlphaFold monomer V2.0 prediction for macrophage mannose receptor 1 (P22897) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P22897
- Elsewhere: RCSB PDB 7L61 · PDBe 7L61 · UniProt P22897
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.