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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

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