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Zinc in PDB 7uac: Human Pro-Meprin Alpha (Zymogen State)

Enzymatic activity of Human Pro-Meprin Alpha (Zymogen State)

All present enzymatic activity of Human Pro-Meprin Alpha (Zymogen State):
3.4.24.18;

Other elements in 7uac:

The structure of Human Pro-Meprin Alpha (Zymogen State) also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Pro-Meprin Alpha (Zymogen State) (pdb code 7uac). 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 Human Pro-Meprin Alpha (Zymogen State), PDB code: 7uac:

Zinc binding site 1 out of 1 in 7uac

Go back to Zinc Binding Sites List in 7uac
Zinc binding site 1 out of 1 in the Human Pro-Meprin Alpha (Zymogen State)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Pro-Meprin Alpha (Zymogen State) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn702

b:92.7
occ:1.00
OD1 H:ASP58 1.6 83.2 1.0
NE2 H:HIS159 2.0 82.5 1.0
NE2 H:HIS165 2.0 82.9 1.0
CG H:ASP58 2.2 83.2 1.0
OD2 H:ASP58 2.3 83.2 1.0
NE2 H:HIS155 2.3 82.3 1.0
CD2 H:HIS159 2.9 82.5 1.0
CE1 H:HIS159 2.9 82.5 1.0
CE1 H:HIS165 2.9 82.9 1.0
CD2 H:HIS165 3.1 82.9 1.0
CD2 H:HIS155 3.1 82.3 1.0
CE1 H:HIS155 3.2 82.3 1.0
CB H:ASP58 3.6 83.2 1.0
ND1 H:HIS159 3.9 82.5 1.0
CG H:HIS159 3.9 82.5 1.0
ND1 H:HIS165 4.0 82.9 1.0
OE1 H:GLU156 4.1 83.0 1.0
CG H:HIS165 4.1 82.9 1.0
CG H:HIS155 4.3 82.3 1.0
ND1 H:HIS155 4.3 82.3 1.0
CA H:ASP58 4.5 83.2 1.0
CG1 H:ILE59 4.7 81.8 1.0
O H:GLN56 4.7 84.3 1.0
N H:ASP58 4.7 83.2 1.0
C H:ASP58 4.8 83.2 1.0
O H:ASP58 4.8 83.2 1.0
CD H:GLU156 5.0 83.0 1.0

Reference:

C.Bayly-Jones, C.J.Lupton, C.Fritz, H.Venugopal, D.Ramsbeck, M.Wermann, C.Jager, A.De Marco, S.Schilling, D.Schlenzig, J.C.Whisstock. Helical Ultrastructure of the Metalloprotease Meprin Alpha in Complex with A Small Molecule Inhibitor. Nat Commun V. 13 6178 2022.
ISSN: ESSN 2041-1723
PubMed: 36261433
DOI: 10.1038/S41467-022-33893-7
Page generated: Wed Oct 30 11:56:29 2024

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