Research workbench
GREEN/CYAN wascfp at pH 2.0
Analyse GREEN/CYAN wascfp at pH 2.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DQM
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- WASCFP_PH2
- Ligands
- CRF
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | WASCFP_PH2 | protein | 227 | 11% helix, 52% strand | — |
Ligands and binding sites
- CRF · [(4Z)-2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(1H-indol-3-ylmethylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.74 | 0.96 | 25 | CRF |
| 2 | 53 | 0.28 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 5DQM · Green/cyan WasCFP at pH 2.0 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 5DQM · PDBe 5DQM
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