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Fluorogen activating protein AM2.2 in complex with TO1-2P

Analyse Fluorogen activating protein AM2.2 in complex with TO1-2P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5J74
Type
protein
Length
464 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Scfv AM2.2
Ligands
6GN, PO4
Pockets
6 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AScfv AM2.2protein2316% helix, 51% strand—
BScfv AM2.2protein2337% helix, 52% strand—

Ligands and binding sites

  • 6GN · 1-(17-amino-5,8-dioxo-12,15-dioxa-4,9-diazaheptadecan-1-yl)-4-{[3-(3-sulfopropyl)-1,3-benzothiazol-3-ium-2-yl]methyl}quinolin-1-ium · ligand · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17080.710.7877empty
22610.570.77296GN
32320.540.77296GN
4800.310.7316empty
5680.290.7318empty

Interfaces

1 interface between chains.

  • A–B · 459 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 5J74 · Fluorogen activating protein AM2.2 in complex with TO1-2p · the same entry in another collection · chain A against A, TM-score 1.00

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