Zinc in PDB 7wg2: Evaa-KLATE1

Enzymatic activity of Evaa-KLATE1

All present enzymatic activity of Evaa-KLATE1:
2.3.2.8;

Protein crystallography data

The structure of Evaa-KLATE1, PDB code: 7wg2 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) 29.49 / 1.76
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.6, 86.6, 161.11, 90, 90, 90
R / Rfree (%) 18 / 21.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Evaa-KLATE1 (pdb code 7wg2). 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 Evaa-KLATE1, PDB code: 7wg2:

Zinc binding site 1 out of 1 in 7wg2

Go back to Zinc Binding Sites List in 7wg2
Zinc binding site 1 out of 1 in the Evaa-KLATE1


Mono view


Stereo pair view

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

b:21.7
occ:1.00
SG A:CYS26 2.3 23.4 1.0
SG A:CYS96 2.3 21.3 1.0
SG A:CYS95 2.3 21.0 1.0
SG A:CYS23 2.4 21.2 1.0
HB2 A:CYS95 3.0 28.9 1.0
HB3 A:CYS26 3.1 29.6 1.0
HB3 A:CYS23 3.2 26.8 1.0
CB A:CYS23 3.2 22.4 1.0
H A:CYS26 3.3 27.2 1.0
HB2 A:CYS96 3.3 23.5 1.0
CB A:CYS95 3.3 24.1 1.0
HB2 A:CYS23 3.3 26.8 1.0
CB A:CYS26 3.3 24.6 1.0
CB A:CYS96 3.4 19.6 1.0
H A:CYS96 3.5 24.0 1.0
HB2 A:TYR25 3.6 27.7 1.0
N A:CYS96 3.6 20.0 1.0
N A:CYS26 3.8 22.7 1.0
HE2 A:LYS30 3.9 30.1 1.0
HB3 A:CYS95 4.0 28.9 1.0
C A:CYS95 4.0 19.9 1.0
HB1 A:ALA19 4.0 30.3 1.0
HB2 A:CYS26 4.1 29.6 1.0
CA A:CYS96 4.1 19.6 1.0
O A:HOH948 4.1 26.4 1.0
CA A:CYS26 4.1 22.5 1.0
HD2 A:TYR25 4.1 30.8 1.0
H A:GLY28 4.2 29.5 1.0
HZ3 A:LYS30 4.2 30.8 1.0
HB3 A:CYS96 4.2 23.5 1.0
CA A:CYS95 4.2 20.8 1.0
HA A:CYS96 4.4 23.5 1.0
H A:TYR25 4.5 25.8 1.0
H A:ASN27 4.5 26.6 1.0
CB A:TYR25 4.5 23.1 1.0
HD21 A:ASN94 4.6 22.5 1.0
CA A:CYS23 4.7 23.2 1.0
CE A:LYS30 4.7 25.1 1.0
H A:CYS95 4.7 23.4 1.0
O A:CYS95 4.7 20.9 1.0
NZ A:LYS30 4.8 25.7 1.0
C A:CYS26 4.8 25.4 1.0
C A:TYR25 4.8 24.9 1.0
N A:ASN27 4.8 22.2 1.0
HE3 A:LYS30 4.8 30.1 1.0
N A:CYS95 4.9 19.5 1.0
HZ2 A:LYS30 4.9 30.8 1.0
HB2 A:SER56 4.9 34.4 1.0
CB A:ALA19 4.9 25.3 1.0
HA A:CYS26 4.9 27.1 1.0
HA A:CYS23 4.9 27.8 1.0
HB2 A:ALA19 4.9 30.3 1.0
HA2 A:GLY28 5.0 28.8 1.0
CD2 A:TYR25 5.0 25.7 1.0
ND2 A:ASN94 5.0 18.8 1.0
HA A:CYS95 5.0 25.0 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 05:18:10 2023

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