Zinc in PDB 7wg4: Dvaa-KLATE1

Enzymatic activity of Dvaa-KLATE1

All present enzymatic activity of Dvaa-KLATE1:
2.3.2.8;

Protein crystallography data

The structure of Dvaa-KLATE1, PDB code: 7wg4 was solved by M.K.Kim, B.H.Kim, S.-J.Oh, H.K.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.57 / 1.51
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.46, 86.46, 160.61, 90, 90, 90
R / Rfree (%) 18.5 / 21.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Dvaa-KLATE1 (pdb code 7wg4). 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 Dvaa-KLATE1, PDB code: 7wg4:

Zinc binding site 1 out of 1 in 7wg4

Go back to Zinc Binding Sites List in 7wg4
Zinc binding site 1 out of 1 in the Dvaa-KLATE1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dvaa-KLATE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:22.1
occ:1.00
HG A:CYS23 1.2 26.6 1.0
HG A:CYS96 1.3 26.2 1.0
HG A:CYS95 1.9 25.6 1.0
SG A:CYS26 2.3 22.3 1.0
SG A:CYS95 2.3 21.3 1.0
SG A:CYS23 2.4 22.2 1.0
SG A:CYS96 2.4 21.8 1.0
HB2 A:CYS95 3.0 27.2 1.0
HB3 A:CYS26 3.1 30.9 1.0
HB3 A:CYS23 3.1 24.6 1.0
CB A:CYS23 3.1 20.5 1.0
HB2 A:CYS23 3.2 24.6 1.0
H A:CYS26 3.3 28.0 1.0
CB A:CYS26 3.3 25.7 1.0
CB A:CYS95 3.3 22.7 1.0
HB2 A:CYS96 3.3 21.9 1.0
CB A:CYS96 3.4 18.2 1.0
H A:CYS96 3.4 21.3 1.0
N A:CYS96 3.6 17.8 1.0
HB2 A:TYR25 3.6 30.3 1.0
N A:CYS26 3.8 23.4 1.0
HE2 A:LYS30 3.9 30.8 1.0
HB3 A:CYS95 4.0 27.2 1.0
HB3 A:ALA19 4.0 27.7 1.0
C A:CYS95 4.0 19.0 1.0
HB2 A:CYS26 4.1 30.9 1.0
CA A:CYS26 4.1 20.9 1.0
CA A:CYS96 4.1 23.3 1.0
O A:HOH934 4.1 27.9 1.0
H A:GLY28 4.2 27.7 1.0
HD2 A:TYR25 4.2 33.8 1.0
CA A:CYS95 4.2 21.2 1.0
HB3 A:CYS96 4.3 21.9 1.0
HZ3 A:LYS30 4.4 31.4 1.0
HA A:CYS96 4.4 27.9 1.0
H A:TYR25 4.4 27.1 1.0
H A:ASN27 4.5 27.3 1.0
HD21 A:ASN94 4.6 21.7 1.0
CB A:TYR25 4.6 25.2 1.0
CE A:LYS30 4.6 25.7 1.0
CA A:CYS23 4.6 20.5 1.0
C A:TYR25 4.7 26.1 1.0
HE3 A:LYS30 4.7 30.8 1.0
H A:CYS95 4.7 24.2 1.0
O A:CYS95 4.8 21.4 1.0
C A:CYS26 4.8 24.7 1.0
HA A:CYS26 4.9 25.1 1.0
N A:ASN27 4.9 22.8 1.0
NZ A:LYS30 4.9 26.2 1.0
CB A:ALA19 4.9 23.1 1.0
N A:CYS95 4.9 20.2 1.0
HB1 A:ALA19 4.9 27.7 1.0
HA A:CYS23 5.0 24.6 1.0
HA2 A:GLY28 5.0 27.9 1.0
HZ2 A:LYS30 5.0 31.4 1.0

Reference:

B.H.Kim, M.K.Kim, S.J.Oh, K.T.Nguyen, J.H.Kim, A.Varshavsky, C.S.Hwang, H.K.Song. Crystal Structure of the ATE1 Arginyl-Trna-Protein Transferase and Arginylation of N-Degron Substrates. Proc.Natl.Acad.Sci.Usa V. 119 97119 2022.
ISSN: ESSN 1091-6490
PubMed: 35878037
DOI: 10.1073/PNAS.2209597119
Page generated: Sat Apr 8 05:18:14 2023

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