Zinc in PDB 8esv: Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab

Enzymatic activity of Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab

All present enzymatic activity of Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab:
3.4.24.81;

Other elements in 8esv:

The structure of Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab (pdb code 8esv). 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 Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab, PDB code: 8esv:

Zinc binding site 1 out of 1 in 8esv

Go back to Zinc Binding Sites List in 8esv
Zinc binding site 1 out of 1 in the Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human ADAM10-TSPAN15 Complex Bound to 11G2 Vfab within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn803

b:77.9
occ:1.00
O1 A:BAT804 1.9 52.2 1.0
O2 A:BAT804 2.1 54.2 1.0
NE2 A:HIS387 2.3 31.8 1.0
NE2 A:HIS393 2.3 33.1 1.0
NE2 A:HIS383 2.3 27.2 1.0
CD2 A:HIS387 2.4 30.7 1.0
C2 A:BAT804 2.6 48.9 1.0
N1 A:BAT804 2.6 51.8 1.0
CD2 A:HIS383 3.1 27.5 1.0
CE1 A:HIS393 3.1 37.0 1.0
CD2 A:HIS393 3.3 31.8 1.0
CE1 A:HIS383 3.4 33.3 1.0
CE1 A:HIS387 3.5 36.9 1.0
CG A:HIS387 3.7 24.7 1.0
C1 A:BAT804 4.0 34.6 1.0
OE2 A:GLU384 4.1 48.1 1.0
ND1 A:HIS387 4.2 32.3 1.0
ND1 A:HIS393 4.3 34.3 1.0
CG A:HIS383 4.3 25.5 1.0
CG A:HIS393 4.4 34.2 1.0
ND1 A:HIS383 4.4 32.2 1.0
C3 A:BAT804 4.5 40.8 1.0
C5 A:BAT804 4.5 43.8 1.0
C8 A:BAT804 4.8 36.6 1.0
CE A:MET417 4.8 38.6 1.0
CB A:HIS387 4.8 27.3 1.0
C9 A:BAT804 4.8 38.6 1.0
C4 A:BAT804 5.0 50.3 1.0

Reference:

C.H.Lipper, E.D.Egan, K.H.Gabriel, S.C.Blacklow. Structural Basis For Selective Proteolysis of ADAM10 Substrates at Membrane-Proximal Sites To Be Published.
Page generated: Fri Jul 28 06:52:53 2023

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