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Zinc in PDB 3d68: Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq)

Enzymatic activity of Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq)

All present enzymatic activity of Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq):
3.4.17.20;

Protein crystallography data

The structure of Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq), PDB code: 3d68 was solved by T.H.C.Brondijk, E.G.Huizinga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.03 / 2.80
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 159.460, 159.460, 139.180, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 23.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq) (pdb code 3d68). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq), PDB code: 3d68:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 3d68

Go back to Zinc Binding Sites List in 3d68
Zinc binding site 1 out of 3 in the Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq)


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 A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:71.2
occ:1.00
 OE1 A:GLU162 2.0 64.4 1.0
ND1 A:HIS288 2.1 61.8 1.0
ND1 A:HIS159 2.2 64.0 1.0
OE2 A:GLU162 2.5 68.2 1.0
CD A:GLU162 2.6 64.3 1.0
CE1 A:HIS288 2.8 65.5 1.0
N A:ARG650 2.9 67.7 1.0
CE1 A:HIS159 3.0 64.5 1.0
CG A:HIS288 3.1 60.9 1.0
CG A:HIS159 3.2 63.1 1.0
CA A:ARG650 3.4 69.8 1.0
CB A:HIS288 3.7 62.2 1.0
CB A:HIS159 3.7 62.8 1.0
NE2 A:HIS288 3.9 64.0 1.0
NE2 A:HIS159 4.1 63.7 1.0
CD2 A:HIS288 4.1 61.3 1.0
CG A:GLU162 4.1 64.1 1.0
C A:ARG650 4.2 70.0 1.0
CD2 A:HIS159 4.2 62.5 1.0
NH1 A:ARG217 4.2 68.6 1.0
O A:SER289 4.3 62.3 1.0
CA A:HIS288 4.4 62.1 1.0
O A:ARG650 4.4 69.4 1.0
N A:SER289 4.6 60.5 1.0
CB A:ARG650 4.7 69.8 1.0
CB A:GLU162 4.9 64.4 1.0
N A:HIS159 5.0 63.6 1.0
CA A:HIS159 5.0 63.0 1.0

Zinc binding site 2 out of 3 in 3d68

Go back to Zinc Binding Sites List in 3d68
Zinc binding site 2 out of 3 in the Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:73.7
occ:1.00
 ND1 B:HIS288 2.0 68.0 1.0
OE1 B:GLU162 2.0 70.2 1.0
ND1 B:HIS159 2.0 67.2 1.0
CD B:GLU162 2.7 69.1 1.0
OE2 B:GLU162 2.7 72.6 1.0
CE1 B:HIS288 2.8 69.7 1.0
CE1 B:HIS159 2.9 71.2 1.0
N B:ARG650 2.9 72.6 1.0
CG B:HIS159 3.1 68.2 1.0
CG B:HIS288 3.1 68.1 1.0
CA B:ARG650 3.4 74.0 1.0
CB B:HIS159 3.5 68.8 1.0
CB B:HIS288 3.6 67.3 1.0
NE2 B:HIS288 3.9 67.6 1.0
NE2 B:HIS159 4.1 68.6 1.0
CG B:GLU162 4.1 69.3 1.0
CD2 B:HIS288 4.1 67.5 1.0
NH1 B:ARG217 4.2 72.2 1.0
CD2 B:HIS159 4.2 69.2 1.0
C B:ARG650 4.2 74.2 1.0
O B:SER289 4.4 66.9 1.0
CA B:HIS288 4.5 66.7 1.0
O B:ARG650 4.5 73.9 1.0
N B:SER289 4.6 65.8 1.0
CB B:ARG650 4.7 74.1 1.0
CA B:HIS159 4.9 69.0 1.0
CZ B:ARG217 4.9 71.9 1.0
CB B:GLU162 4.9 69.3 1.0
N B:HIS159 4.9 68.9 1.0

Zinc binding site 3 out of 3 in 3d68

Go back to Zinc Binding Sites List in 3d68
Zinc binding site 3 out of 3 in the Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of A T325I/T329I/H333Y/H335Q Mutant of Thrombin- Activatable Fibrinolysis Inhibitor (Tafi-Iiyq) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn501

b:69.0
occ:1.00
 ND1 C:HIS159 1.9 68.1 1.0
ND1 C:HIS288 2.1 66.0 1.0
OE1 C:GLU162 2.2 68.4 1.0
OE2 C:GLU162 2.6 69.8 1.0
CE1 C:HIS159 2.7 69.8 1.0
N C:ARG650 2.7 65.1 1.0
CD C:GLU162 2.7 65.3 1.0
CG C:HIS288 3.0 64.7 1.0
CG C:HIS159 3.1 68.4 1.0
CE1 C:HIS288 3.1 64.1 1.0
CA C:ARG650 3.2 68.0 1.0
CB C:HIS288 3.3 63.6 1.0
CB C:HIS159 3.6 67.5 1.0
NE2 C:HIS159 3.9 67.5 1.0
C C:ARG650 4.1 68.8 1.0
CD2 C:HIS159 4.1 70.6 1.0
CD2 C:HIS288 4.1 63.3 1.0
NE2 C:HIS288 4.1 63.0 1.0
CA C:HIS288 4.2 63.6 1.0
CG C:GLU162 4.2 65.3 1.0
NH1 C:ARG217 4.3 68.2 1.0
O C:SER289 4.4 63.8 1.0
O C:ARG650 4.4 69.0 1.0
CB C:ARG650 4.4 68.0 1.0
N C:SER289 4.6 63.3 1.0
N C:HIS159 4.8 69.0 1.0
CA C:HIS159 4.9 68.0 1.0
OXT C:ARG650 5.0 69.5 1.0

Reference:

P.F.Marx, T.H.Brondijk, T.Plug, R.A.Romijn, W.Hemrika, J.C.M.Meijers, E.G.Huizinga. Crystal Structures of Tafi Elucidate the Inactivation Mechanism of Activated Tafi: A Novel Mechanism For Enzyme Autoregulation Blood V. 112 2803 2008.
ISSN: ISSN 0006-4971
PubMed: 18559974
DOI: 10.1182/BLOOD-2008-03-146001
Page generated: Thu Oct 24 12:04:05 2024

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