Research workbench
Modified mtfp* for enhanced metal binding: co-crystallization with CUCL2
Analyse Modified mtfp* for enhanced metal binding: co-crystallization with CUCL2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R6D
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GFP-like fluorescent chromoprotein CFP484
- UniProt
- Q9U6Y3
- Ligands
- PIA, CU
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GFP-like fluorescent chromoprotein CFP484 | protein | 213 | 4% helix, 57% strand | Q9U6Y3 |
Ligands and binding sites
- PIA · [(4Z)-2-[(1S)-1-aminoethyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid · ligand · chains A
- CU · Copper (II) ion · metal · 2 copies · 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 | 61 | 0.71 | 0.97 | 25 | PIA |
| 2 | 68 | 0.33 | 0.76 | 23 | CU |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 4R6D · Modified mTFP* for enhanced metal binding: co-crystallization with CuCl2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9U6Y3 · AlphaFold monomer V2.0 prediction for GFP-like fluorescent chromoprotein CFP484 (Q9U6Y3) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9U6Y3
- Elsewhere: RCSB PDB 4R6D · PDBe 4R6D · UniProt Q9U6Y3
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