Zinc in PDB 8a7d: Partial Dimer Complex of Papp-A and Its Inhibitor STC2

Enzymatic activity of Partial Dimer Complex of Papp-A and Its Inhibitor STC2

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

Other elements in 8a7d:

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

Calcium (Ca) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Partial Dimer Complex of Papp-A and Its Inhibitor STC2 (pdb code 8a7d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Partial Dimer Complex of Papp-A and Its Inhibitor STC2, PDB code: 8a7d:

Zinc binding site 1 out of 1 in 8a7d

Go back to Zinc Binding Sites List in 8a7d
Zinc binding site 1 out of 1 in the Partial Dimer Complex of Papp-A and 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 Partial Dimer Complex of Papp-A and Its Inhibitor STC2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1708

b:101.9
occ:1.00
CE1 C:HIS572 2.3 74.0 1.0
NE2 C:HIS566 2.3 65.7 1.0
NE2 C:HIS572 2.3 75.4 1.0
NE2 C:HIS562 2.3 64.3 1.0
CD2 C:LEU525 2.8 102.9 1.0
CD2 C:HIS566 2.8 61.2 1.0
CD2 C:HIS562 3.2 64.4 1.0
CE1 C:HIS562 3.3 69.2 1.0
CE1 C:HIS566 3.5 60.9 1.0
ND1 C:HIS572 3.6 73.2 1.0
CD2 C:HIS572 3.6 74.3 1.0
CG C:LEU525 3.9 104.8 1.0
CD1 C:LEU525 4.0 102.7 1.0
NE2 C:GLN563 4.0 67.1 1.0
CG C:HIS566 4.1 54.6 1.0
CG C:HIS572 4.2 73.5 1.0
ND1 C:HIS566 4.4 50.5 1.0
CG C:HIS562 4.4 60.2 1.0
ND1 C:HIS562 4.4 65.5 1.0
CE1 C:TYR638 4.5 105.1 1.0
OH C:TYR638 4.6 106.8 1.0
CD C:GLN563 4.8 62.6 1.0
OE1 C:GLN563 4.9 65.5 1.0

Reference:

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
Page generated: Sat Apr 8 07:32:47 2023

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