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Sfgfp double mutant - 133/149 P-ethynyl-L-phenylalanine

Analyse Sfgfp double mutant - 133/149 P-ethynyl-L-phenylalanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DPJ
Type
protein
Length
898 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein
UniProt
A0A059PIQ0
Ligands
CRO
Pockets
12 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 10% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGreen fluorescent proteinprotein22611% helix, 52% strandA0A059PIQ0
B, CGreen fluorescent proteinprotein2249% helix, 52% strandA0A059PIQ0
DGreen fluorescent proteinprotein22410% helix, 52% 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 · 4 copies · chains A, B, C, D

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

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1950.770.9825CRO
2870.760.9829CRO
3850.760.9821CRO
4880.760.9827CRO
59250.740.7889empty

Interfaces

4 interfaces between chains.

  • C–D · 972 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 929 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 293 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 170 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 cofactor, 8 modified (chromophore, nonstandard).

Compared structures

  • 5DPJ · sfGFP double mutant - 133/149 p-ethynyl-L-phenylalanine · the same entry in another collection · chain C against C, TM-score 1.00

Analyse

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