Research workbench
Mouse ECD with Fab1
Analyse Mouse ECD with Fab1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O9H
- Type
- protein
- Length
- 1,034 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Homo sapiens; Mus musculus
- Molecule
- Heavy chain; Light chain; Gastric inhibitory polypeptide receptor
- UniProt
- Q0P543
- Ligands
- NA
- Pockets
- 11 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.1 · 5 distinct chains · 8% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Heavy chain | protein | 213 | 6% helix, 53% strand | — |
| L | Light chain | protein | 214 | 6% helix, 53% strand | — |
| A | Heavy chain | protein | 210 | 6% helix, 53% strand | — |
| B | Light chain | protein | 217 | 5% helix, 52% strand | — |
| D, C | Gastric inhibitory polypeptide receptor | protein | 90 | 28% helix, 24% strand | Q0P543 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, C, H, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 928 | 0.81 | 0.83 | 95 | empty |
| 2 | 737 | 0.75 | 0.80 | 70 | empty |
| 3 | 1138 | 0.74 | 0.77 | 126 | empty |
| 4 | 138 | 0.49 | 0.78 | 19 | empty |
| 5 | 74 | 0.47 | 0.83 | 22 | empty |
Interfaces
9 interfaces between chains.
- H–L · 1875 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1794 Ų buried · 15 hydrogen bonds · protein-protein
- H–B · 785 Ų buried · 12 hydrogen bonds · protein-protein
- H–D · 560 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 515 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
Compared structures
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 Q0P543
- Elsewhere: RCSB PDB 6O9H · PDBe 6O9H · UniProt Q0P543
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