Research workbench
C-type carbohydrate-recognition domain 4 of the mannose receptor
Analyse C-type carbohydrate-recognition domain 4 of the mannose receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L68
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrophage mannose receptor 1
- UniProt
- P22897
- Ligands
- CA
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage mannose receptor 1 | protein | 133 | 23% helix, 28% strand | P22897 |
| B | Macrophage mannose receptor 1 | protein | 135 | 24% helix, 27% strand | P22897 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.53 | 0.82 | 26 | empty |
| 2 | 185 | 0.53 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 663 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 7L68 · C-type carbohydrate-recognition domain 4 of the mannose receptor · 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 0.92
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 7L68 · PDBe 7L68 · UniProt P22897
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