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Zinc in PDB 1pyt: Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C

Enzymatic activity of Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C

All present enzymatic activity of Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C:
3.4.17.1;

Protein crystallography data

The structure of Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C, PDB code: 1pyt was solved by F.X.Gomis-Ruth, M.Gomez, W.Bode, R.Huber, F.X.Aviles, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.35
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 188.500, 188.500, 82.500, 90.00, 90.00, 120.00
R / Rfree (%) 19.2 / 28.3

Other elements in 1pyt:

The structure of Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C (pdb code 1pyt). 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 Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C, PDB code: 1pyt:

Zinc binding site 1 out of 1 in 1pyt

Go back to Zinc Binding Sites List in 1pyt
Zinc binding site 1 out of 1 in the Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ternary Complex of Procarboxypeptidase A, Proproteinase E, and Chymotrypsinogen C within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn350

b:36.5
occ:1.00
 O B:HOH351 1.3 35.3 1.0
OE2 B:GLU72 2.0 32.7 1.0
ND1 B:HIS196 2.1 34.1 1.0
OE1 B:GLU72 2.1 31.0 1.0
ND1 B:HIS69 2.2 34.1 1.0
CD B:GLU72 2.4 29.6 1.0
CG B:HIS196 3.1 34.4 1.0
CG B:HIS69 3.2 32.9 1.0
CE1 B:HIS196 3.2 33.9 1.0
CE1 B:HIS69 3.3 33.6 1.0
CB B:HIS69 3.4 31.7 1.0
CB B:HIS196 3.4 34.1 1.0
CG B:GLU72 3.9 29.3 1.0
O B:HOH377 4.0 29.4 1.0
CA B:HIS196 4.2 35.3 1.0
CD2 B:HIS196 4.3 33.3 1.0
N B:SER197 4.3 37.2 1.0
NE2 B:HIS196 4.3 33.0 1.0
O B:SER197 4.3 39.1 1.0
CD2 B:HIS69 4.4 33.3 1.0
NE2 B:HIS69 4.4 34.1 1.0
O B:HOH425 4.4 49.2 1.0
O B:HOH364 4.5 41.6 1.0
OE2 B:GLU270 4.6 40.3 1.0
O B:HOH426 4.6 53.0 1.0
CA B:HIS69 4.7 31.5 1.0
C B:HIS196 4.8 36.2 1.0
CB B:GLU72 4.8 27.1 1.0
NH2 B:ARG127 4.8 31.8 1.0
N B:HIS69 4.8 32.6 1.0
OE1 B:GLU270 5.0 39.3 1.0

Reference:

F.X.Gomis-Ruth, M.Gomez, W.Bode, R.Huber, F.X.Aviles. The Three-Dimensional Structure of the Native Ternary Complex of Bovine Pancreatic Procarboxypeptidase A with Proproteinase E and Chymotrypsinogen C. Embo J. V. 14 4387 1995.
ISSN: ISSN 0261-4189
PubMed: 7556081
Page generated: Wed Oct 16 17:58:22 2024

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