Zinc in PDB 2abz: Crystal Structure of C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A

All present enzymatic activity of Crystal Structure of C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A:
3.4.17.1;

The structure of Crystal Structure of C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A, PDB code: 2abz was solved by J.L.Arolas, G.M.Popowicz, S.Bronsoms, F.X.Aviles, R.Huber, T.A.Holak, S.Ventura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.16
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	124.930, 124.930, 154.980, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 23.4

The binding sites of Zinc atom in the Crystal Structure of C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A (pdb code 2abz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A, PDB code: 2abz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A


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 C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:23.1 occ:1.00 OE2 A:GLU72 2.1 21.9 1.0 ND1 A:HIS69 2.1 20.9 1.0 ND1 A:HIS196 2.1 23.3 1.0 O C:VAL66 2.4 20.7 1.0 C C:VAL66 2.6 20.0 1.0 CD A:GLU72 2.7 23.5 1.0 OE1 A:GLU72 2.7 24.5 1.0 CE1 A:HIS69 3.0 21.0 1.0 CE1 A:HIS196 3.0 24.1 1.0 CG A:HIS196 3.1 23.4 1.0 CG A:HIS69 3.2 20.8 1.0 CB A:HIS196 3.5 22.5 1.0 CB A:HIS69 3.5 20.6 1.0 CA C:VAL66 4.0 20.0 1.0 NH2 A:ARG127 4.1 20.8 1.0 NE2 A:HIS196 4.2 24.8 1.0 CG A:GLU72 4.2 21.8 1.0 NE2 A:HIS69 4.2 22.6 1.0 CD2 A:HIS196 4.2 24.0 1.0 CD2 A:HIS69 4.3 21.5 1.0 O A:SER197 4.3 23.4 1.0 CA A:HIS196 4.4 22.6 1.0 N A:SER197 4.7 23.0 1.0 OE2 A:GLU270 4.7 27.1 1.0 N C:VAL66 4.8 20.1 1.0 CA A:HIS69 4.9 20.9 1.0 CZ A:ARG127 4.9 20.1 1.0 OE1 A:GLU270 5.0 28.3 1.0 CG2 A:ILE68 5.0 24.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A


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 C19A/C43A Mutant of Leech Carboxypeptidase Inhibitor in Complex with Bovine Carboxypeptidase A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:21.1 occ:1.00 OE2 B:GLU72 2.0 16.1 1.0 ND1 B:HIS196 2.1 16.9 1.0 ND1 B:HIS69 2.1 20.1 1.0 OE1 B:GLU72 2.6 16.9 1.0 O E:VAL66 2.6 19.5 1.0 CD B:GLU72 2.6 16.6 1.0 C E:VAL66 2.7 19.0 1.0 CE1 B:HIS196 3.0 19.4 1.0 CE1 B:HIS69 3.0 20.3 1.0 CG B:HIS196 3.1 19.1 1.0 CG B:HIS69 3.2 19.3 1.0 CB B:HIS196 3.5 18.8 1.0 CB B:HIS69 3.6 19.2 1.0 CA E:VAL66 4.1 18.2 1.0 NH2 B:ARG127 4.1 13.4 1.0 CG B:GLU72 4.1 16.8 1.0 NE2 B:HIS196 4.2 19.6 1.0 NE2 B:HIS69 4.2 19.9 1.0 CD2 B:HIS196 4.2 19.9 1.0 CD2 B:HIS69 4.3 20.4 1.0 O B:SER197 4.3 19.3 1.0 CA B:HIS196 4.3 19.4 1.0 N B:SER197 4.7 18.7 1.0 OE2 B:GLU270 4.7 22.2 1.0 CA B:HIS69 4.9 19.3 1.0 N E:VAL66 4.9 18.2 1.0 N B:HIS69 5.0 20.0 1.0 CG2 B:ILE68 5.0 20.8 1.0 CZ B:ARG127 5.0 14.6 1.0

J.L.Arolas, G.M.Popowicz, S.Bronsoms, F.X.Aviles, R.Huber, T.A.Holak, S.Ventura. Study of A Major Intermediate in the Oxidative Folding of Leech Carboxypeptidase Inhibitor: Contribution of the Fourth Disulfide Bond J.Mol.Biol. V. 352 961 2005.
ISSN: ISSN 0022-2836
PubMed: 16126224
DOI: 10.1016/J.JMB.2005.07.065