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Zinc in PDB 4a6e: Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin

Enzymatic activity of Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin

All present enzymatic activity of Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin:
2.1.1.4;

Protein crystallography data

The structure of Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin, PDB code: 4a6e was solved by P.Legrand, A.Haouz, W.Shepard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.74 / 2.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 170.080, 170.080, 128.220, 90.00, 90.00, 120.00
R / Rfree (%) 16.33 / 21.22

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin (pdb code 4a6e). 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 Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin, PDB code: 4a6e:

Zinc binding site 1 out of 1 in 4a6e

Go back to Zinc Binding Sites List in 4a6e
Zinc binding site 1 out of 1 in the Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human N-Acetylserotonin Methyltransferase (Asmt) in Complex with Sam and N-Acetylserotonin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1348

b:88.2
occ:1.00
 NE2 A:HIS271 2.2 64.3 1.0
OE1 A:GLU267 2.6 86.2 1.0
O A:HOH2033 2.7 76.1 1.0
O A:HOH2048 2.8 72.1 1.0
O A:HOH2047 2.9 49.0 1.0
CE1 A:HIS271 3.2 63.7 1.0
CD2 A:HIS271 3.2 63.3 1.0
CD A:GLU267 3.9 95.2 1.0
ND1 A:HIS271 4.3 63.0 1.0
CG A:HIS271 4.3 59.8 1.0
O A:ALA324 4.6 60.3 1.0
OE2 A:GLU267 4.7 88.0 1.0
CB A:GLU267 4.8 56.9 1.0
CG A:GLU267 4.8 68.7 1.0
CD2 A:TYR270 5.0 55.3 1.0

Reference:

H.G.Botros, P.Legrand, C.Pagan, V.Bondet, P.Weber, M.Ben-Abdallah, N.Lemiere, G.Huguet, J.Bellalou, E.Maronde, P.Beguin, A.Haouz, W.Shepard, T.Bourgeron. Crystal Structure and Functional Mapping of Human Asmt, the Last Enzyme of the Melatonin Synthesis Pathway. J.Pineal Res. V. 54 46 2013.
ISSN: ISSN 0742-3098
PubMed: 22775292
DOI: 10.1111/J.1600-079X.2012.01020.X
Page generated: Wed Dec 16 05:02:26 2020

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