Research workbench
Crystal structure of the CysR-CTLD2 fragment of human MR at acidic pH (pH 4.6)
Analyse Crystal structure of the CysR-CTLD2 fragment of human MR at acidic pH (pH 4.6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6INU
- Type
- protein
- Length
- 898 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.65
- Source
- Homo sapiens
- Molecule
- Macrophage mannose receptor 1
- UniProt
- P22897
- Pockets
- 12 · best druggability 0.74
Structure
x-ray diffraction · resolution 2.65 · 2 distinct chains · 13% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage mannose receptor 1 | protein | 468 | 13% helix, 34% strand | P22897 |
| B | Macrophage mannose receptor 1 | protein | 430 | 14% helix, 30% strand | P22897 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 700 | 0.74 | 0.80 | 70 | empty |
| 2 | 156 | 0.54 | 0.79 | 15 | empty |
| 3 | 132 | 0.50 | 0.80 | 30 | empty |
| 4 | 224 | 0.50 | 0.75 | 30 | empty |
| 5 | 249 | 0.50 | 0.75 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 572 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 6INU · Crystal structure of the cysr-CTLD2 fragment of human mr at acidic pH (pH 4.6) · 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 B against A, TM-score 0.91
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 6INU · PDBe 6INU · UniProt P22897
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.