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Zinc in PDB 2ctc: The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate

Enzymatic activity of The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate

All present enzymatic activity of The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate:
3.4.17.1;

Protein crystallography data

The structure of The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate, PDB code: 2ctc was solved by A.Teplyakov, K.S.Wilson, P.Orioli, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.600, 60.270, 47.250, 90.00, 97.27, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate (pdb code 2ctc). 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 The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate, PDB code: 2ctc:

Zinc binding site 1 out of 1 in 2ctc

Go back to Zinc Binding Sites List in 2ctc
Zinc binding site 1 out of 1 in the The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The High Resolution Crystal Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn308

b:8.9
occ:1.00
 O A:HOH338 2.0 15.4 1.0
ND1 A:HIS69 2.1 8.2 1.0
ND1 A:HIS196 2.1 8.1 1.0
OE2 A:GLU72 2.3 11.2 1.0
OE1 A:GLU72 2.3 8.8 1.0
CD A:GLU72 2.7 7.6 1.0
CE1 A:HIS69 3.0 9.9 1.0
CE1 A:HIS196 3.1 7.5 1.0
CG A:HIS69 3.1 6.0 1.0
CG A:HIS196 3.2 8.0 1.0
CB A:HIS69 3.4 6.9 1.0
CB A:HIS196 3.5 7.2 1.0
O A:HOH389 3.9 28.4 1.0
OA A:HFA309 4.1 18.8 1.0
O A:SER197 4.1 8.5 1.0
O A:HOH313 4.2 9.9 1.0
NE2 A:HIS69 4.2 7.7 1.0
CG A:GLU72 4.2 7.4 1.0
NE2 A:HIS196 4.2 9.7 1.0
CD2 A:HIS69 4.2 7.4 1.0
O A:HOH362 4.3 21.3 1.0
CA A:HIS196 4.3 7.1 1.0
CD2 A:HIS196 4.3 7.5 1.0
O A:HFA309 4.5 13.1 1.0
NH1 A:ARG127 4.5 21.4 1.0
N A:SER197 4.5 6.4 1.0
CA A:HFA309 4.6 21.5 1.0
C A:HFA309 4.7 18.0 1.0
CA A:HIS69 4.7 5.0 1.0
OE1 A:GLU270 4.9 26.5 1.0
C A:HIS196 4.9 6.6 1.0
N A:HIS69 4.9 6.0 1.0
OE2 A:GLU270 5.0 27.3 1.0

Reference:

A.Teplyakov, K.S.Wilson, P.Orioli, S.Mangani. High-Resolution Structure of the Complex Between Carboxypeptidase A and L-Phenyl Lactate. Acta Crystallogr.,Sect.D V. 49 534 1993.
ISSN: ISSN 0907-4449
PubMed: 15299490
DOI: 10.1107/S0907444993007267
Page generated: Wed Dec 16 03:20:10 2020

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