Zinc in PDB 8a7e: Papp-A Dimer in Complex with Its Inhibitor STC2

All present enzymatic activity of Papp-A Dimer in Complex with Its Inhibitor STC2:
3.4.24.79;

The structure of Papp-A Dimer in Complex with Its Inhibitor STC2 also contains other interesting chemical elements:

Calcium

(Ca)

16 atoms

The binding sites of Zinc atom in the Papp-A Dimer in Complex with Its Inhibitor STC2 (pdb code 8a7e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Papp-A Dimer in Complex with Its Inhibitor STC2, PDB code: 8a7e:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Papp-A Dimer in Complex with Its Inhibitor STC2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Papp-A Dimer in Complex with Its Inhibitor STC2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1701 b:311.8 occ:1.00 NE2 C:HIS572 2.3 269.7 1.0 NE2 C:HIS566 2.3 222.5 1.0 NE2 C:HIS562 2.3 253.6 1.0 CE1 C:HIS566 2.5 222.5 1.0 CD2 C:LEU525 2.8 308.3 1.0 CE1 C:HIS572 2.8 269.7 1.0 CD1 C:LEU525 2.8 308.3 1.0 OH C:TYR638 2.8 296.0 1.0 CE1 C:TYR638 3.2 296.0 1.0 CG C:LEU525 3.2 308.3 1.0 CE1 C:HIS562 3.2 253.6 1.0 CD2 C:HIS562 3.3 253.6 1.0 CZ C:TYR638 3.5 296.0 1.0 CD2 C:HIS566 3.5 222.5 1.0 CD2 C:HIS572 3.6 269.7 1.0 ND1 C:HIS566 3.7 222.5 1.0 ND1 C:HIS572 4.1 269.7 1.0 CG C:HIS566 4.3 222.5 1.0 ND1 C:HIS562 4.4 253.6 1.0 CG C:HIS562 4.4 253.6 1.0 CD1 C:TYR638 4.5 296.0 1.0 CG C:HIS572 4.5 269.7 1.0 CB C:LEU525 4.7 308.3 1.0 CE2 C:TYR638 4.8 296.0 1.0 OE1 C:GLN563 4.8 237.4 1.0

Zinc binding site 2 out of 2 in the Papp-A Dimer in Complex with Its Inhibitor STC2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Papp-A Dimer in Complex with Its Inhibitor STC2 within 5.0Å range: probe atom residue distance (Å) B Occ Q:Zn1701 b:310.7 occ:1.00 NE2 Q:HIS572 2.3 270.2 1.0 NE2 Q:HIS566 2.3 224.4 1.0 NE2 Q:HIS562 2.3 254.8 1.0 CD1 Q:LEU525 2.5 303.8 1.0 CD2 Q:LEU525 2.5 303.8 1.0 CG Q:LEU525 2.8 303.8 1.0 CE1 Q:HIS572 2.8 270.2 1.0 CE1 Q:TYR638 2.9 295.6 1.0 OH Q:TYR638 3.0 295.6 1.0 CD2 Q:HIS562 3.1 254.8 1.0 CE1 Q:HIS566 3.1 224.4 1.0 CE1 Q:HIS562 3.3 254.8 1.0 CZ Q:TYR638 3.4 295.6 1.0 CD2 Q:HIS566 3.4 224.4 1.0 CD2 Q:HIS572 3.6 270.2 1.0 CD1 Q:TYR638 4.1 295.6 1.0 ND1 Q:HIS572 4.1 270.2 1.0 CG Q:HIS562 4.2 254.8 1.0 ND1 Q:HIS562 4.2 254.8 1.0 CB Q:LEU525 4.3 303.8 1.0 ND1 Q:HIS566 4.3 224.4 1.0 CG Q:HIS572 4.5 270.2 1.0 CG Q:HIS566 4.5 224.4 1.0 OE1 Q:GLN563 4.6 235.3 1.0 CE2 Q:TYR638 4.8 295.6 1.0 NE2 Q:GLN563 4.8 235.3 1.0

S.D.Kobbero, M.Gajhede, O.A.Mirza, S.Kloverpris, T.R.Kjaer, J.H.Mikkelsen, T.Boesen, C.Oxvig. Structure of the Proteolytic Enzyme Papp-A with the Endogenous Inhibitor Stanniocalcin-2 Reveals Its Inhibitory Mechanism. Nat Commun V. 13 6084 2022.
ISSN: ESSN 2041-1723
PubMed: 36257932
DOI: 10.1038/S41467-022-33698-8