Atomistry » Zinc » PDB 3czn-3d7g » 3d4u
Atomistry »
  Zinc »
    PDB 3czn-3d7g »
      3d4u »

Zinc in PDB 3d4u: Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor.

Enzymatic activity of Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor.

All present enzymatic activity of Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor.:
3.4.17.20;

Protein crystallography data

The structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor., PDB code: 3d4u was solved by L.Sanglas, Z.Valnickova, J.L.Arolas, I.Pallares, T.Guevara, M.Sola, T.Kristensen, J.J.Enghild, F.X.Aviles, F.X.Gomis-Ruth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.08 / 1.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 84.200, 84.200, 127.900, 90.00, 90.00, 120.00
R / Rfree (%) 15.6 / 17.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor. (pdb code 3d4u). 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 Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor., PDB code: 3d4u:

Zinc binding site 1 out of 1 in 3d4u

Go back to Zinc Binding Sites List in 3d4u
Zinc binding site 1 out of 1 in the Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bovine Thrombin-Activatable Fibrinolysis Inhibitor (Tafia) in Complex with Tick-Derived Carboxypeptidase Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn309

b:16.2
occ:1.00
 OE2 A:GLU72 2.0 14.5 1.0
ND1 A:HIS196 2.1 16.5 1.0
ND1 A:HIS69 2.1 13.4 1.0
O B:LEU74 2.1 14.4 1.0
OXT B:LEU74 2.5 13.1 1.0
C B:LEU74 2.6 14.4 1.0
CD A:GLU72 2.7 15.3 1.0
OE1 A:GLU72 2.8 16.0 1.0
CE1 A:HIS196 2.9 16.6 1.0
CE1 A:HIS69 3.0 15.8 1.0
CG A:HIS69 3.2 14.4 1.0
CG A:HIS196 3.2 15.9 1.0
CB A:HIS69 3.5 15.7 1.0
CB A:HIS196 3.6 15.0 1.0
NH1 A:ARG127 4.0 14.8 1.0
O B:HOH516 4.1 14.9 1.0
CA B:LEU74 4.1 14.0 1.0
NE2 A:HIS196 4.1 15.8 1.0
NE2 A:HIS69 4.2 14.7 1.0
CG A:GLU72 4.2 14.9 1.0
CD2 A:HIS196 4.2 14.7 1.0
CD2 A:HIS69 4.2 14.8 1.0
O A:SER197 4.3 15.2 1.0
CH3 A:ACT601 4.4 15.3 1.0
C A:ACT601 4.4 15.2 1.0
CA A:HIS196 4.5 14.9 1.0
O A:ACT601 4.5 14.6 1.0
O A:HOH2372 4.6 16.8 1.0
N A:SER197 4.8 15.0 1.0
OE2 A:GLU270 4.8 17.1 1.0
N B:LEU74 4.8 14.2 1.0
CA A:HIS69 4.9 14.9 1.0
CG2 A:ILE68 4.9 20.3 1.0
CZ A:ARG127 4.9 16.4 1.0
OXT A:ACT601 4.9 14.2 1.0

Reference:

L.Sanglas, Z.Valnickova, J.L.Arolas, I.Pallares, T.Guevara, M.Sola, T.Kristensen, J.J.Enghild, F.X.Aviles, F.X.Gomis-Ruth. Structure of Activated Thrombin-Activatable Fibrinolysis Inhibitor, A Molecular Link Between Coagulation and Fibrinolysis. Mol.Cell V. 31 598 2008.
ISSN: ISSN 1097-2765
PubMed: 18722183
DOI: 10.1016/J.MOLCEL.2008.05.031
Page generated: Thu Oct 24 12:02:56 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy