Research workbench
Crystal structure of full-length split GFP mutant D117C disulfide dimer, P 64 2 2 space group
Analyse Crystal structure of full-length split GFP mutant D117C disulfide dimer, P 64 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W6O
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluorescent protein D117C
- Ligands
- CRO
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fluorescent protein D117C | protein | 204 | 5% helix, 50% strand | — |
Ligands and binding sites
- CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-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
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.79 | 0.97 | 31 | CRO |
| 2 | 77 | 0.40 | 0.79 | 21 | empty |
| 3 | 55 | 0.37 | 0.80 | 13 | empty |
| 4 | 54 | 0.36 | 0.79 | 12 | empty |
Modifications
Observed in the structure: 2 cofactor (chromophore).
Compared structures
- 4W6O · Crystal Structure of Full-Length Split GFP Mutant D117C Disulfide Dimer, P 64 2 2 Space… · 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 4W6O · PDBe 4W6O
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