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Zinc in PDB 3osl: Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor

Enzymatic activity of Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor

All present enzymatic activity of Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor:
3.4.17.20;

Protein crystallography data

The structure of Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor, PDB code: 3osl was solved by Z.Valnickova, L.Sanglas, J.L.Arolas, S.V.Petersen, C.Schar, D.Otzen, F.X.Aviles, F.X.Gomis-Ruth, J.J.Enghild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 6.00
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 279.100, 279.100, 279.100, 90.00, 90.00, 90.00
R / Rfree (%) 31.3 / 32

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor (pdb code 3osl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor, PDB code: 3osl:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3osl

Go back to Zinc Binding Sites List in 3osl
Zinc binding site 1 out of 2 in the Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn999

b:22.2
occ:1.00
OE2 A:GLU184 2.0 21.3 1.0
ND1 A:HIS310 2.1 21.3 1.0
ND1 A:HIS181 2.1 19.0 1.0
O B:LEU74 2.4 17.2 1.0
C B:LEU74 2.5 17.5 1.0
CD A:GLU184 2.7 21.6 1.0
OE1 A:GLU184 2.8 21.5 1.0
CE1 A:HIS310 2.9 20.9 1.0
CE1 A:HIS181 3.0 21.7 1.0
CG A:HIS181 3.2 20.0 1.0
CG A:HIS310 3.2 20.5 1.0
CB A:HIS181 3.5 21.2 1.0
CB A:HIS310 3.6 20.6 1.0
CA B:LEU74 4.0 16.7 1.0
NH1 A:ARG239 4.0 23.6 1.0
NE2 A:HIS310 4.1 19.6 1.0
NE2 A:HIS181 4.1 20.9 1.0
CG A:GLU184 4.2 22.1 1.0
CD2 A:HIS310 4.2 18.6 1.0
CD2 A:HIS181 4.2 20.7 1.0
O A:SER311 4.3 24.2 1.0
CA A:HIS310 4.5 20.1 1.0
N A:SER311 4.8 22.3 1.0
OE2 A:GLU385 4.8 26.2 1.0
CB B:LEU74 4.9 16.3 1.0
N B:LEU74 4.9 16.4 1.0
CA A:HIS181 4.9 20.2 1.0
CG2 A:ILE180 4.9 23.2 1.0
CZ A:ARG239 4.9 25.6 1.0

Zinc binding site 2 out of 2 in 3osl

Go back to Zinc Binding Sites List in 3osl
Zinc binding site 2 out of 2 in the Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Bovine Thrombin-Activatable Fibrinolysis Inhibitor in Complex with Tick Carboxypeptidase Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn999

b:20.9
occ:1.00
OE2 C:GLU184 2.0 19.8 1.0
ND1 C:HIS310 2.1 20.4 1.0
ND1 C:HIS181 2.1 17.6 1.0
O D:LEU74 2.3 40.6 1.0
C D:LEU74 2.5 40.9 1.0
CD C:GLU184 2.7 20.2 1.0
OE1 C:GLU184 2.8 20.2 1.0
CE1 C:HIS310 2.9 20.0 1.0
CE1 C:HIS181 3.0 20.3 1.0
CG C:HIS181 3.2 18.6 1.0
CG C:HIS310 3.2 19.8 1.0
CB C:HIS181 3.5 19.7 1.0
CB C:HIS310 3.6 19.8 1.0
CA D:LEU74 4.0 40.2 1.0
NH1 C:ARG239 4.0 21.8 1.0
NE2 C:HIS310 4.1 18.9 1.0
NE2 C:HIS181 4.2 19.4 1.0
CG C:GLU184 4.2 20.6 1.0
CD2 C:HIS310 4.2 18.1 1.0
CD2 C:HIS181 4.2 19.2 1.0
O C:SER311 4.3 22.8 1.0
CA C:HIS310 4.5 19.4 1.0
N C:SER311 4.8 21.3 1.0
OE2 C:GLU385 4.8 25.3 1.0
N D:LEU74 4.8 40.4 1.0
CA C:HIS181 4.9 18.8 1.0
CG2 C:ILE180 4.9 22.4 1.0
CB D:LEU74 4.9 40.2 1.0
CZ C:ARG239 4.9 23.7 1.0

Reference:

Z.Valnickova, L.Sanglas, J.L.Arolas, S.V.Petersen, C.Schar, D.Otzen, F.X.Aviles, F.X.Gomis-Ruth, J.J.Enghild. Flexibility of the Thrombin-Activatable Fibrinolysis Inhibitor Pro-Domain Enables Productive Binding of Protein Substrates. J.Biol.Chem. V. 285 38243 2010.
ISSN: ISSN 0021-9258
PubMed: 20880845
DOI: 10.1074/JBC.M110.150342
Page generated: Wed Dec 16 04:41:13 2020

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