Research workbench
Crystal structure of full-length split GFP mutant D21H/K26C disulfide and metal-mediated dimer, P 21 21 21 space group, form 3
Analyse Crystal structure of full-length split GFP mutant D21H/K26C disulfide and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W77
- Type
- protein
- Length
- 432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluorescent protein D21H/K26C
- Ligands
- CU
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fluorescent protein D21H/K26C | protein | 215 | 9% helix, 53% strand | — |
| B | Fluorescent protein D21H/K26C | protein | 217 | 6% helix, 54% strand | — |
Ligands and binding sites
- CU · Copper (II) ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.80 | 0.97 | 29 | empty |
| 2 | 123 | 0.79 | 0.97 | 32 | empty |
| 3 | 219 | 0.52 | 0.77 | 25 | empty |
| 4 | 118 | 0.38 | 0.74 | 16 | empty |
| 5 | 74 | 0.36 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 355 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4W77 · Crystal Structure of Full-Length Split GFP Mutant D21H/K26C Disulfide and Metal-Mediated… · 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 4W77 · PDBe 4W77
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