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Zinc in PDB 3d6n: Crystal Structure of Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase

Enzymatic activity of Crystal Structure of Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase

All present enzymatic activity of Crystal Structure of Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase:
2.1.3.2; 3.5.2.3;

Protein crystallography data

The structure of Crystal Structure of Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase, PDB code: 3d6n was solved by B.F.P.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.00 / 2.30
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 158.439, 158.439, 233.553, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 20.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase (pdb code 3d6n). 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 Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase, PDB code: 3d6n:

Zinc binding site 1 out of 1 in 3d6n

Go back to Zinc Binding Sites List in 3d6n
Zinc binding site 1 out of 1 in the Crystal Structure of Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase


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 Aquifex Dihydroorotase Activated By Aspartate Transcarbamoylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn423

b:54.4
occ:1.00
OG1 A:FLC424 2.1 46.5 1.0
NE2 A:HIS63 2.2 38.1 1.0
NE2 A:HIS61 2.3 34.7 1.0
OD1 A:ASP153 2.4 46.9 1.0
OD1 A:ASP305 2.7 42.7 1.0
CGC A:FLC424 2.9 45.7 1.0
OD2 A:ASP153 3.0 51.1 1.0
CG A:ASP153 3.0 44.0 1.0
CE1 A:HIS63 3.1 37.1 1.0
CD2 A:HIS61 3.2 32.2 1.0
CE1 A:HIS61 3.3 33.6 1.0
CD2 A:HIS63 3.3 36.6 1.0
CG A:FLC424 3.4 39.6 1.0
CG A:ASP305 3.6 41.2 1.0
OG2 A:FLC424 3.8 50.1 1.0
O A:HOH577 4.0 54.3 1.0
OD2 A:ASP305 4.0 45.7 1.0
CG A:MET93 4.1 29.9 1.0
ND1 A:HIS63 4.2 40.1 1.0
ND1 A:HIS61 4.4 37.4 1.0
CG A:HIS63 4.4 36.0 1.0
CG A:HIS61 4.4 34.2 1.0
CB A:FLC424 4.5 39.7 1.0
CB A:ASP153 4.5 40.3 1.0
CA A:FLC424 4.5 38.7 1.0
NE2 A:HIS232 4.7 50.6 1.0
CB A:ASP305 4.8 37.2 1.0
OA1 A:FLC424 4.8 37.4 1.0
OB2 A:FLC424 4.8 33.2 1.0
SD A:MET93 4.9 34.3 1.0
CB A:MET93 4.9 29.4 1.0
CD2 A:HIS232 4.9 50.7 1.0
OE1 A:GLN231 5.0 45.5 1.0

Reference:

P.Zhang, P.D.Martin, C.Purcarea, A.Vaishnav, J.S.Brunzelle, R.Fernando, H.I.Guy-Evans, D.R.Evans, B.F.Edwards. Dihydroorotase From the Hyperthermophile Aquifiex Aeolicus Is Activated By Stoichiometric Association with Aspartate Transcarbamoylase and Forms A One-Pot Reactor For Pyrimidine Biosynthesis. Biochemistry V. 48 766 2009.
ISSN: ISSN 0006-2960
PubMed: 19128030
DOI: 10.1021/BI801831R
Page generated: Wed Dec 16 04:12:13 2020

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