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Zinc in PDB 7p2k: Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain.

Enzymatic activity of Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain.

All present enzymatic activity of Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain.:
2.3.2.27;

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain. (pdb code 7p2k). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain., PDB code: 7p2k:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7p2k

Go back to Zinc Binding Sites List in 7p2k
Zinc binding site 1 out of 2 in the Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn70

b:0.4
occ:1.00
ND1 A:HIS40 2.1 0.3 1.0
SG A:CYS20 2.1 0.5 1.0
SG A:CYS43 2.2 0.5 1.0
SG A:CYS17 2.2 0.6 1.0
HB2 A:HIS40 3.0 0.2 1.0
HB3 A:CYS20 3.1 0.6 1.0
CE1 A:HIS40 3.1 0.3 1.0
CG A:HIS40 3.2 0.2 1.0
CB A:CYS20 3.3 0.6 1.0
H A:HIS40 3.3 0.3 1.0
CB A:CYS43 3.4 0.5 1.0
HE1 A:HIS40 3.4 0.5 1.0
H A:CYS20 3.4 0.5 1.0
HB2 A:CYS43 3.4 0.4 1.0
CB A:CYS17 3.5 0.6 1.0
HB2 A:CYS17 3.5 0.7 1.0
HB3 A:CYS43 3.6 0.6 1.0
CB A:HIS40 3.6 0.3 1.0
HB3 A:CYS17 3.8 0.7 1.0
HB3 A:PHE39 3.8 0.3 1.0
HB A:ILE19 3.8 0.6 1.0
HB2 A:CYS20 4.0 0.6 1.0
HB3 A:SER22 4.1 0.7 1.0
N A:CYS20 4.1 0.6 1.0
N A:HIS40 4.2 0.3 1.0
NE2 A:HIS40 4.3 0.3 1.0
HD22 A:LEU24 4.3 1.2 1.0
CD2 A:HIS40 4.3 0.3 1.0
CA A:CYS20 4.3 0.6 1.0
HB3 A:HIS40 4.4 0.3 1.0
CA A:HIS40 4.6 0.3 1.0
HG21 A:ILE19 4.6 1.5 1.0
HD21 A:LEU24 4.7 1.3 1.0
CA A:CYS43 4.7 0.6 1.0
CA A:CYS17 4.8 0.7 1.0
CB A:ILE19 4.8 0.6 1.0
H A:LEU21 4.8 0.7 1.0
CB A:PHE39 4.8 0.3 1.0
H A:CYS43 4.8 0.4 1.0
HA A:CYS17 4.8 0.7 1.0
HA A:CYS43 4.9 0.7 1.0
CD2 A:LEU24 5.0 0.5 1.0
HB2 A:SER22 5.0 0.7 1.0

Zinc binding site 2 out of 2 in 7p2k

Go back to Zinc Binding Sites List in 7p2k
Zinc binding site 2 out of 2 in the Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution uc(Nmr) Structure of Arginine to Cysteine Mutant of Arkadia Ring Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn71

b:0.7
occ:1.00
O A:CYS35 1.8 1.0 1.0
SG A:CYS57 2.2 1.3 1.0
ND1 A:HIS37 2.2 0.6 1.0
SG A:CYS35 2.2 1.6 1.0
SG A:CYS54 2.3 0.7 1.0
HB2 A:CYS35 2.9 0.9 1.0
C A:CYS35 2.9 0.7 1.0
CB A:CYS35 3.0 0.7 1.0
CE1 A:HIS37 3.2 0.7 1.0
HB2 A:HIS37 3.2 0.6 1.0
H A:CYS57 3.2 0.7 1.0
CG A:HIS37 3.3 0.6 1.0
HE1 A:HIS37 3.3 0.8 1.0
CA A:CYS35 3.5 0.6 1.0
HB2 A:CYS57 3.5 1.5 1.0
CB A:CYS57 3.6 0.9 1.0
HG3 A:MET36 3.6 3.4 1.0
HG2 A:MET36 3.8 3.4 1.0
CB A:HIS37 3.8 0.6 1.0
CB A:CYS54 3.8 0.6 1.0
HB A:ILE56 3.8 0.8 1.0
HB2 A:CYS54 3.9 0.6 1.0
HB3 A:CYS35 4.0 1.0 1.0
HA A:CYS35 4.0 0.8 1.0
N A:MET36 4.0 0.6 1.0
N A:CYS57 4.1 0.8 1.0
HB3 A:CYS54 4.2 0.6 1.0
CG A:MET36 4.2 2.1 1.0
HB3 A:CYS57 4.3 1.9 1.0
NE2 A:HIS37 4.3 0.8 1.0
N A:HIS37 4.4 0.7 1.0
H A:ILE56 4.4 0.8 1.0
CD2 A:HIS37 4.4 0.7 1.0
HD12 A:ILE56 4.4 1.7 1.0
C A:MET36 4.4 0.7 1.0
H A:HIS37 4.5 0.7 1.0
CA A:CYS57 4.5 0.9 1.0
HD2 A:PRO55 4.5 1.4 1.0
HB3 A:HIS37 4.6 0.6 1.0
N A:CYS35 4.6 0.6 1.0
CA A:MET36 4.7 0.7 1.0
H A:CYS35 4.7 0.7 1.0
CA A:HIS37 4.8 0.6 1.0
H A:MET36 4.9 0.7 1.0
O A:MET36 4.9 0.7 1.0
CB A:ILE56 4.9 0.8 1.0

Reference:

M.Birkou, V.Raptis, K.D.Marousis, A.Tsevis, K.Bourikas, D.Bentrop, V.Episkopou, G.A.Spyroulias. Impact of A Single Nucleotide Polymorphism on the 3D Protein Structure and Ubiquitination Activity of E3 Ubiquitin Ligase Arkadia. Front Mol Biosci V. 9 44129 2022.
ISSN: ESSN 2296-889X
PubMed: 35281275
DOI: 10.3389/FMOLB.2022.844129
Page generated: Sat Apr 8 01:13:22 2023

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