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Crystal structure of anopheles gambiae SER/THR phosphatase complexed with ZN2+

Analyse Crystal structure of anopheles gambiae SER/THR phosphatase complexed with ZN2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2I0O
Type
protein
Length
287 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SER/THR phosphatase
UniProt
Q7PP01
Ligands
ZN
Pockets
1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASER/THR phosphataseprotein28732% helix, 32% strandQ7PP01

Ligands and binding sites

  • ZN · Zinc ion · metal · 6 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1630.270.7317empty

Compared structures

  • 2I0O · Crystal structure of Anopheles gambiae Ser/Thr phosphatase complexed with Zn2+ · the same entry in another collection · chain A against A, TM-score 1.00

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