Atomistry » Zinc » PDB 5g2u-5gl7 » 5g2u
Atomistry »
  Zinc »
    PDB 5g2u-5gl7 »
      5g2u »

Zinc in PDB 5g2u: Structure of BT1596,A 2-O Gag Sulfatase

Enzymatic activity of Structure of BT1596,A 2-O Gag Sulfatase

All present enzymatic activity of Structure of BT1596,A 2-O Gag Sulfatase:
3.1.6.18;

Protein crystallography data

The structure of Structure of BT1596,A 2-O Gag Sulfatase, PDB code: 5g2u was solved by A.Cartmell, E.C.Lowe, A.Basle, L.I.Crouch, M.Czjzek, J.Turnbull, B.Henrissat, N.Terrapon, S.Thomas, H.Murray, S.J.Firbank, D.N.Bolam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.87 / 1.43
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 68.872, 68.872, 110.004, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 16

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of BT1596,A 2-O Gag Sulfatase (pdb code 5g2u). 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 Structure of BT1596,A 2-O Gag Sulfatase, PDB code: 5g2u:

Zinc binding site 1 out of 1 in 5g2u

Go back to Zinc Binding Sites List in 5g2u
Zinc binding site 1 out of 1 in the Structure of BT1596,A 2-O Gag Sulfatase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of BT1596,A 2-O Gag Sulfatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1487

b:20.3
occ:1.00
ND1 A:HIS477 2.1 21.5 1.0
NE2 A:HIS470 2.1 18.3 1.0
SG A:CYS233 2.2 19.6 1.0
SG A:CYS234 2.3 22.2 1.0
CE1 A:HIS477 3.0 21.6 1.0
CE1 A:HIS470 3.1 19.5 1.0
CD2 A:HIS470 3.1 21.7 1.0
CG A:HIS477 3.2 17.4 1.0
N A:CYS234 3.2 17.4 1.0
CB A:CYS233 3.3 18.4 1.0
CB A:CYS234 3.5 21.1 1.0
C A:CYS233 3.5 17.3 1.0
CB A:HIS477 3.5 19.1 1.0
CA A:CYS234 3.6 19.3 1.0
CA A:CYS233 3.9 17.2 1.0
O A:CYS233 4.0 20.1 1.0
CA A:HIS477 4.0 19.5 1.0
NE2 A:HIS477 4.1 21.6 1.0
ND1 A:HIS470 4.2 20.7 1.0
CD2 A:HIS477 4.3 21.6 1.0
CG A:HIS470 4.3 21.5 1.0
CD1 A:TYR231 4.3 19.5 1.0
N A:CYS233 4.5 16.8 1.0
O A:TYR231 4.7 19.8 1.0
CA A:TYR231 4.8 17.0 1.0
N A:HIS477 4.9 19.6 1.0
C A:TYR231 5.0 18.9 1.0

Reference:

A.Cartmell, E.C.Lowe, A.Basle, S.J.Firbank, D.A.Ndeh, H.Murray, N.Terrapon, V.Lombard, B.Henrissat, J.E.Turnbull, M.Czjzek, H.J.Gilbert, D.N.Bolam. How Members of the Human Gut Microbiota Overcome the Sulfation Problem Posed By Glycosaminoglycans. Proc. Natl. Acad. Sci. V. 114 7037 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28630303
DOI: 10.1073/PNAS.1704367114
Page generated: Sun Oct 27 16:53:54 2024

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy