Research workbench
Crystal structure of ECGP123, an extremely thermostable green fluorescent protein
Analyse Crystal structure of ECGP123, an extremely thermostable green fluorescent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TZG
- Type
- protein
- Length
- 1,749 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluorescent protein
- Ligands
- CRQ
- Pockets
- 19 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 5% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fluorescent protein | protein | 218 | 4% helix, 57% strand | — |
| B, C, D, F, G, H | Fluorescent protein | protein | 219 | 5% helix, 57% strand | — |
| E | Fluorescent protein | protein | 217 | 6% helix, 57% strand | — |
Ligands and binding sites
- CRQ · [2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 861 | 0.85 | 0.88 | 89 | empty |
| 2 | 93 | 0.77 | 0.98 | 27 | CRQ |
| 3 | 87 | 0.76 | 0.98 | 26 | CRQ |
| 4 | 77 | 0.75 | 0.98 | 25 | CRQ |
| 5 | 80 | 0.75 | 0.98 | 26 | CRQ |
Interfaces
15 interfaces between chains.
- C–E · 1542 Ų buried · 24 hydrogen bonds · protein-protein
- B–F · 1541 Ų buried · 31 hydrogen bonds · protein-protein
- A–G · 1537 Ų buried · 21 hydrogen bonds · protein-protein
- D–H · 1526 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 975 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 cofactor (chromophore).
Compared structures
- 4TZG · Crystal structure of eCGP123, an extremely thermostable green fluorescent protein · 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 4TZG · PDBe 4TZG
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