Zinc in PDB 1f57: Carboxypeptidase A Complex with D-Cysteine at 1.75 A

All present enzymatic activity of Carboxypeptidase A Complex with D-Cysteine at 1.75 A:
3.4.17.1;

The structure of Carboxypeptidase A Complex with D-Cysteine at 1.75 A, PDB code: 1f57 was solved by D.M.Van Aalten, C.R.Chong, L.Joshua-Tor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.78 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.389, 57.712, 58.193, 90.00, 101.62, 90.00
R / Rfree (%)	13.7 / 16.4

The binding sites of Zinc atom in the Carboxypeptidase A Complex with D-Cysteine at 1.75 A (pdb code 1f57). 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 Carboxypeptidase A Complex with D-Cysteine at 1.75 A, PDB code: 1f57:

Zinc binding site 1 out of 1 in the Carboxypeptidase A Complex with D-Cysteine at 1.75 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carboxypeptidase A Complex with D-Cysteine at 1.75 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn310 b:11.3 occ:1.00 ND1 A:HIS69 2.1 7.1 1.0 ND1 A:HIS196 2.1 7.8 1.0 SG A:DCY308 2.2 13.9 1.0 OE1 A:GLU72 2.3 12.1 1.0 OE2 A:GLU72 2.3 11.9 1.0 CD A:GLU72 2.6 10.2 1.0 CE1 A:HIS69 3.0 9.8 1.0 CE1 A:HIS196 3.1 11.1 1.0 CG A:HIS69 3.1 6.5 1.0 CG A:HIS196 3.1 9.9 1.0 CB A:DCY308 3.3 16.2 1.0 CB A:HIS196 3.4 9.0 1.0 CB A:HIS69 3.5 7.1 1.0 O A:SER197 4.1 9.1 1.0 O A:HOH402 4.1 10.3 1.0 NE2 A:HIS69 4.1 10.1 1.0 CG A:GLU72 4.2 5.5 1.0 NE2 A:HIS196 4.2 8.4 1.0 CD2 A:HIS69 4.2 7.3 1.0 CD2 A:HIS196 4.2 9.3 1.0 O A:HOH432 4.3 17.6 1.0 CA A:HIS196 4.3 7.3 1.0 O A:HOH560 4.3 30.5 1.0 NH1 A:ARG127 4.4 14.1 1.0 N A:SER197 4.5 9.6 1.0 CA A:DCY308 4.5 20.3 1.0 O A:DCY308 4.5 16.3 1.0 C A:DCY308 4.6 24.6 1.0 O A:HOH559 4.6 29.4 1.0 CA A:HIS69 4.8 4.1 1.0 C A:HIS196 5.0 6.1 1.0 N A:HIS69 5.0 7.9 1.0

D.M.Van Aalten, C.R.Chong, L.Joshua-Tor. Crystal Structure of Carboxypeptidase A Complexed with D-Cysteine at 1.75 A - Inhibitor-Induced Conformational Changes. Biochemistry V. 39 10082 2000.
ISSN: ISSN 0006-2960
PubMed: 10955996
DOI: 10.1021/BI000952H