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Zinc in PDB 3axt: Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine

Enzymatic activity of Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine

All present enzymatic activity of Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine:
2.1.1.32;

Protein crystallography data

The structure of Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine, PDB code: 3axt was solved by Ihsanawati, T.Sengoku, S.Yokoyama, Y.Bessho, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.41 / 2.49
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 54.438, 140.928, 119.038, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 22.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine (pdb code 3axt). 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 Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine, PDB code: 3axt:

Zinc binding site 1 out of 1 in 3axt

Go back to Zinc Binding Sites List in 3axt
Zinc binding site 1 out of 1 in the Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Complex Structure of Trna Methyltransferase TRM1 From Aquifex Aeolicus with S-Adenosyl-L-Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:96.1
occ:1.00
 SG A:CYS250 2.3 70.7 1.0
SG A:CYS269 2.3 97.6 1.0
SG A:CYS247 2.3 61.1 1.0
SG A:CYS266 2.3 0.5 1.0
CB A:CYS266 3.3 70.2 1.0
CB A:CYS247 3.4 38.5 1.0
CB A:CYS250 3.5 47.5 1.0
CB A:CYS269 3.7 91.7 1.0
N A:CYS269 3.8 93.9 1.0
N A:CYS250 3.8 57.0 1.0
CA A:CYS250 4.2 51.4 1.0
CA A:CYS269 4.3 92.8 1.0
CB A:HIS268 4.3 0.6 1.0
CB A:ASN249 4.5 78.7 1.0
CB A:ASN252 4.6 42.3 1.0
CB A:SER271 4.6 76.6 1.0
N A:GLY270 4.6 89.0 1.0
CA A:CYS266 4.7 72.1 1.0
N A:SER271 4.7 79.0 1.0
CA A:CYS247 4.7 37.1 1.0
C A:CYS269 4.8 93.8 1.0
C A:ASN249 4.8 67.0 1.0
C A:HIS268 4.8 98.8 1.0
C A:CYS250 4.8 46.6 1.0
CD2 A:HIS268 4.8 0.6 1.0
N A:MET251 4.9 45.7 1.0
CA A:HIS268 4.9 97.9 1.0
N A:ASN252 4.9 42.2 1.0
OG A:SER271 5.0 79.9 1.0
N A:HIS268 5.0 93.4 1.0
CG A:HIS268 5.0 0.8 1.0
CA A:ASN249 5.0 71.8 1.0

Reference:

T.Awai, A.Ochi, Ihsanawati, T.Sengoku, A.Hirata, Y.Bessho, S.Yokoyama, H.Hori. Substrate Trna Recognition Mechanism of A Multisite-Specific Trna Methyltransferase, Aquifex Aeolicus TRM1, Based on the X-Ray Crystal Structure J.Biol.Chem. V. 286 35236 2011.
ISSN: ISSN 0021-9258
PubMed: 21844194
DOI: 10.1074/JBC.M111.253641
Page generated: Wed Dec 16 04:07:55 2020

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