GL1X · GenesisL1 explorer

Research workbench

Sfgfp mutant - 149 P-cyano-L-phenylalanine

Analyse Sfgfp mutant - 149 P-cyano-L-phenylalanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DPH
Type
protein
Length
456 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein
UniProt
A0A059PIQ0
Ligands
CRO, MG, CO2
Pockets
4 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGreen fluorescent proteinprotein2248% helix, 52% strandA0A059PIQ0
BGreen fluorescent proteinprotein23211% helix, 51% strandA0A059PIQ0

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 · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 7 copies · chains A, B
  • CO2 · Carbon dioxide · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11460.810.9729CRO, CO2
21270.790.9725CRO, CO2
31390.460.7726MG
4850.310.7222empty

Interfaces

1 interface between chains.

  • A–B · 1212 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor, 2 modified (chromophore, nonstandard).

Compared structures

  • 5DPH · sfGFP mutant - 149 p-cyano-L-phenylalanine · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.