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Zinc in PDB 3fju: Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1

Enzymatic activity of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1

All present enzymatic activity of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1:
3.4.17.1;

Protein crystallography data

The structure of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1, PDB code: 3fju was solved by L.Sanglas, F.X.Aviles, R.Huber, F.X.Gomis-Ruth, J.L.Arolas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.37 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.470, 78.700, 84.500, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 20

Other elements in 3fju:

The structure of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 also contains other interesting chemical elements:

Arsenic (As) 4 atoms
Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 (pdb code 3fju). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 10 binding sites of Zinc where determined in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1, PDB code: 3fju:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 10 in 3fju

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Zinc binding site 1 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn999

b:6.6
occ:1.00
 OE1 A:GLU72 2.0 6.8 1.0
O B:LEU67 2.1 7.4 1.0
ND1 A:HIS69 2.1 5.2 1.0
ND1 A:HIS196 2.1 5.5 1.0
OXT B:LEU67 2.4 7.5 1.0
C B:LEU67 2.6 7.4 1.0
CD A:GLU72 2.7 5.2 1.0
OE2 A:GLU72 2.9 5.9 1.0
CE1 A:HIS196 3.0 5.1 1.0
CE1 A:HIS69 3.0 6.5 1.0
CG A:HIS69 3.1 5.5 1.0
CG A:HIS196 3.2 5.8 1.0
CB A:HIS69 3.5 6.2 1.0
CB A:HIS196 3.5 5.1 1.0
O A:HOH816 3.9 7.0 1.0
NH2 A:ARG127 4.0 6.3 1.0
CA B:LEU67 4.1 7.2 1.0
NE2 A:HIS196 4.2 7.0 1.0
NE2 A:HIS69 4.2 5.9 1.0
CG A:GLU72 4.2 5.5 1.0
CD2 A:HIS69 4.2 6.1 1.0
CD2 A:HIS196 4.3 5.1 1.0
O A:SER197 4.3 6.7 1.0
CH3 A:ACT515 4.3 7.3 1.0
OXT A:ACT515 4.5 7.2 1.0
C A:ACT515 4.5 7.2 1.0
CA A:HIS196 4.5 6.3 1.0
O A:HOH764 4.6 7.9 1.0
OE1 A:GLU270 4.8 10.2 1.0
N B:LEU67 4.8 7.1 1.0
CA A:HIS69 4.8 6.4 1.0
OE2 A:GLU270 4.9 7.7 1.0
N A:SER197 4.9 6.7 1.0
CZ A:ARG127 4.9 6.5 1.0

Zinc binding site 2 out of 10 in 3fju

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Zinc binding site 2 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:10.3
occ:1.00
 O A:ACT519 2.0 19.3 1.0
ND1 A:HIS120 2.1 8.1 1.0
O A:HOH647 2.1 15.7 1.0
C A:ACT519 2.3 17.4 1.0
OXT A:ACT519 2.5 18.0 1.0
CE1 A:HIS120 3.0 9.1 1.0
CG A:HIS120 3.1 7.8 1.0
CH3 A:ACT519 3.3 16.5 1.0
CB A:HIS120 3.5 8.2 1.0
CA A:HIS120 4.0 8.0 1.0
NE2 A:HIS120 4.2 7.9 1.0
CH2 A:TRP73 4.2 6.6 1.0
CD2 A:HIS120 4.2 6.9 1.0
O A:HOH770 4.3 17.1 1.0
O A:HIS120 4.7 8.3 1.0
CG2 A:THR14 4.7 8.7 1.0
C A:HIS120 4.8 8.4 1.0
CZ2 A:TRP73 4.9 6.6 1.0
CZ3 A:TRP73 5.0 7.2 1.0

Zinc binding site 3 out of 10 in 3fju

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Zinc binding site 3 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:14.2
occ:1.00
 O1 A:CAC513 1.7 20.9 1.0
ND1 A:HIS303 2.0 8.2 1.0
OXT A:ACT518 2.0 19.8 1.0
O A:HOH716 2.1 15.3 1.0
O A:ACT518 2.7 16.7 1.0
C A:ACT518 2.8 17.4 1.0
CE1 A:HIS303 2.9 6.8 1.0
CG A:HIS303 3.1 8.8 1.0
AS A:CAC513 3.3 17.8 1.0
O A:HOH719 3.4 18.1 1.0
CB A:HIS303 3.5 8.6 1.0
C1 A:CAC513 4.0 18.0 1.0
NE2 A:HIS303 4.1 7.6 1.0
O2 A:CAC513 4.1 22.8 1.0
CE1 A:HIS307 4.2 12.2 1.0
CD2 A:HIS303 4.2 8.6 1.0
CA A:HIS303 4.2 9.3 1.0
O A:HOH717 4.2 15.6 1.0
CH3 A:ACT518 4.2 18.3 1.0
CD1 A:LEU222 4.4 9.1 1.0
O A:HOH718 4.7 19.9 1.0
C2 A:CAC513 4.7 16.4 1.0
ND1 A:HIS307 4.9 10.3 1.0
NE2 A:HIS307 4.9 13.3 1.0
N A:HIS303 5.0 9.6 1.0

Zinc binding site 4 out of 10 in 3fju

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Zinc binding site 4 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn503

b:17.5
occ:1.00
 O2 A:CAC513 1.9 22.8 1.0
NE2 A:HIS307 2.1 13.3 1.0
O A:HOH688 2.4 8.7 1.0
CE1 A:HIS307 3.0 12.2 1.0
CD2 A:HIS307 3.2 12.7 1.0
AS A:CAC513 3.4 17.8 1.0
O1 A:CAC513 4.0 20.9 1.0
CE1 A:HIS303 4.1 6.8 1.0
ND1 A:HIS307 4.2 10.3 1.0
C2 A:CAC513 4.2 16.4 1.0
CG A:HIS307 4.3 11.9 1.0
O A:HOH718 4.3 19.9 1.0
NE2 A:HIS303 4.7 7.6 1.0
O A:HOH850 4.8 18.8 1.0
ND1 A:HIS303 4.9 8.2 1.0
C1 A:CAC513 5.0 18.0 1.0

Zinc binding site 5 out of 10 in 3fju

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Zinc binding site 5 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn505

b:10.2
occ:1.00
 OE2 A:GLU16 1.9 8.5 1.0
OD1 A:ASP20 1.9 9.3 1.0
O1 A:CAC514 1.9 11.4 1.0
CG A:ASP20 2.8 9.3 1.0
CD A:GLU16 2.8 9.5 1.0
OD2 A:ASP20 3.0 9.6 1.0
OE1 A:GLU16 3.0 9.8 1.0
AS A:CAC514 3.3 15.0 1.0
O A:HOH920 3.7 21.4 1.0
O A:HOH726 3.8 19.3 1.0
C2 A:CAC514 3.9 13.3 1.0
O2 A:CAC514 4.0 15.3 1.0
CG A:GLU16 4.2 9.9 1.0
CB A:ASP20 4.2 7.5 1.0
O A:GLU16 4.5 7.3 1.0
O A:HOH776 4.6 12.1 1.0
C1 A:CAC514 4.9 13.9 1.0

Zinc binding site 6 out of 10 in 3fju

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Zinc binding site 6 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn506

b:14.6
occ:0.95
 O1 A:CAC511 1.8 16.6 0.9
O1 A:CAC512 1.8 15.8 0.9
O A:HOH525 2.0 18.7 0.9
AS A:CAC511 3.2 19.6 0.9
AS A:CAC512 3.2 18.3 0.9
O2 A:CAC512 3.5 14.9 0.9
C2 A:CAC511 3.8 18.2 0.9
O2 A:CAC511 3.9 19.5 0.9
ZN A:ZN507 4.3 15.6 0.9
C1 A:CAC512 4.3 15.9 0.9
C2 A:CAC512 4.7 16.3 0.9
C1 A:CAC511 4.8 18.5 0.9

Zinc binding site 7 out of 10 in 3fju

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Zinc binding site 7 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn507

b:15.6
occ:0.95
 O2 A:CAC512 1.9 14.9 0.9
O2 A:CAC511 1.9 19.5 0.9
O A:ACT517 2.0 14.5 0.9
NE2 A:HIS31 2.0 17.3 1.0
OXT A:ACT517 2.8 15.5 0.9
C A:ACT517 2.8 15.2 0.9
CD2 A:HIS31 2.9 15.8 1.0
CE1 A:HIS31 3.1 17.4 1.0
AS A:CAC512 3.3 18.3 0.9
AS A:CAC511 3.3 19.6 0.9
C2 A:CAC512 3.8 16.3 0.9
C2 A:CAC511 3.8 18.2 0.9
O A:HOH1014 3.9 29.3 1.0
O1 A:CAC512 3.9 15.8 0.9
O A:HOH937 4.0 22.0 1.0
O1 A:CAC511 4.1 16.6 0.9
CG A:HIS31 4.1 15.2 1.0
ND1 A:HIS31 4.1 16.9 1.0
CH3 A:ACT517 4.3 15.7 0.9
CG A:PRO30 4.3 11.6 1.0
ZN A:ZN506 4.3 14.6 0.9
C1 A:CAC512 4.8 15.9 0.9
C1 A:CAC511 4.9 18.5 0.9
O A:HOH525 5.0 18.7 0.9

Zinc binding site 8 out of 10 in 3fju

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Zinc binding site 8 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn508

b:29.2
occ:0.80
 OD1 A:ASP5 2.1 19.2 1.0
O A:HOH524 2.1 10.6 0.8
O A:HOH521 2.2 19.9 0.8
O A:HOH522 2.3 24.1 0.8
OD2 A:ASP5 2.5 18.3 1.0
CG A:ASP5 2.6 15.9 1.0
CB A:ASP5 4.1 14.1 1.0
NZ A:LYS84 4.1 10.8 1.0
O A:HOH722 4.3 22.2 1.0

Zinc binding site 9 out of 10 in 3fju

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Zinc binding site 9 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn509

b:26.4
occ:0.85
 O2 A:CAC514 1.9 15.3 1.0
OE2 A:GLU17 2.3 12.4 1.0
O A:HOH765 2.8 28.4 1.0
O A:HOH773 2.9 25.4 1.0
CD A:GLU17 3.1 10.1 1.0
CG A:GLU17 3.2 8.7 1.0
AS A:CAC514 3.4 15.0 1.0
O A:HOH1006 3.6 28.7 1.0
C1 A:CAC514 3.9 13.9 1.0
O A:HOH768 3.9 10.8 1.0
O A:HOH775 4.1 30.4 1.0
O A:HOH726 4.2 19.3 1.0
OE1 A:GLU17 4.3 9.4 1.0
C2 A:CAC514 4.3 13.3 1.0
OE1 A:GLU16 4.6 9.8 1.0
CB A:GLU17 4.7 6.8 1.0
O1 A:CAC514 4.7 11.4 1.0
O A:HOH917 4.8 23.9 1.0
O A:HOH729 5.0 16.6 1.0

Zinc binding site 10 out of 10 in 3fju

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Zinc binding site 10 out of 10 in the Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Ascaris Suum Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase A1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn504

b:32.2
occ:0.90
 O B:HOH740 2.1 15.8 1.0
NE2 B:HIS38 2.3 14.7 1.0
O B:HOH873 2.6 26.3 1.0
OE1 B:GLU37 2.6 20.2 1.0
O B:HOH1078 3.0 33.0 1.0
CE1 B:HIS38 3.2 14.8 1.0
CD2 B:HIS38 3.3 14.3 1.0
CD B:GLU37 3.6 21.0 1.0
O B:HOH700 3.9 13.6 1.0
NH1 B:ARG33 4.0 14.5 1.0
CB B:GLU37 4.1 14.7 1.0
ND1 B:HIS38 4.3 13.9 1.0
OE2 B:GLU37 4.3 24.5 1.0
CG B:HIS38 4.4 13.4 1.0
CG B:GLU37 4.4 17.9 1.0
CZ2 B:TRP64 4.6 9.6 1.0
O B:HOH633 5.0 15.5 1.0

Reference:

L.Sanglas, F.X.Aviles, R.Huber, F.X.Gomis-Ruth, J.L.Arolas. Mammalian Metallopeptidase Inhibition at the Defense Barrier of Ascaris Parasite Proc.Natl.Acad.Sci.Usa V. 106 1743 2009.
ISSN: ISSN 0027-8424
PubMed: 19179285
DOI: 10.1073/PNAS.0812623106
Page generated: Thu Oct 24 13:14:05 2024

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