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Zinc in PDB 1hee: Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A

Enzymatic activity of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A

All present enzymatic activity of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A:
3.4.17.1;

Protein crystallography data

The structure of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A, PDB code: 1hee was solved by J.H.Cho, N.-C.Ha, S.J.Chung, D.H.Kim, K.Y.Choi, B.-H.Oh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100 / 1.75
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 65.570, 60.524, 74.410, 90.00, 97.84, 90.00
R / Rfree (%) 19.8 / 22.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A (pdb code 1hee). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A, PDB code: 1hee:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1hee

Go back to Zinc Binding Sites List in 1hee
Zinc binding site 1 out of 4 in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 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 Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1308

b:10.6
occ:1.00
 O1 A:LHY1309 2.0 17.6 1.0
OE2 A:GLU72 2.1 6.9 1.0
ND1 A:HIS69 2.1 8.6 1.0
ND1 A:HIS196 2.2 6.6 1.0
OE1 A:GLU72 2.5 7.8 1.0
CD A:GLU72 2.6 6.6 1.0
C1 A:LHY1309 3.1 17.8 1.0
CE1 A:HIS69 3.1 7.7 1.0
CG A:HIS69 3.1 8.6 1.0
CG A:HIS196 3.1 5.2 1.0
CE1 A:HIS196 3.2 8.7 1.0
CB A:HIS196 3.4 5.7 1.0
CB A:HIS69 3.4 6.8 1.0
N2 A:LHY1309 3.7 18.8 1.0
N A:LHY1309 4.1 14.4 1.0
O A:HOH2040 4.1 8.5 1.0
O A:HOH2041 4.1 8.5 1.0
CG A:GLU72 4.1 5.1 1.0
NH1 A:ARG127 4.2 5.8 1.0
NE2 A:HIS69 4.2 8.7 1.0
O A:SER197 4.2 5.3 1.0
CD2 A:HIS69 4.3 8.1 1.0
CD2 A:HIS196 4.3 6.8 1.0
NE2 A:HIS196 4.3 6.9 1.0
CA A:HIS196 4.3 5.5 1.0
CA A:LHY1309 4.3 13.9 1.0
C A:LHY1309 4.4 12.3 1.0
OXT A:LHY1309 4.4 10.8 1.0
N A:SER197 4.6 6.5 1.0
CA A:HIS69 4.8 7.2 1.0
O A:LHY1309 4.8 12.3 1.0
N A:HIS69 5.0 5.5 1.0
CZ A:ARG127 5.0 8.0 1.0
CG2 A:ILE68 5.0 8.0 1.0

Zinc binding site 2 out of 4 in 1hee

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Zinc binding site 2 out of 4 in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 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 Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1308

b:9.9
occ:1.00
 O1 B:LHY1309 2.1 19.5 1.0
ND1 B:HIS69 2.1 6.8 1.0
OE2 B:GLU72 2.2 5.4 1.0
ND1 B:HIS196 2.2 4.6 1.0
OE1 B:GLU72 2.5 6.5 1.0
CD B:GLU72 2.7 5.6 1.0
C1 B:LHY1309 3.0 19.9 1.0
CE1 B:HIS69 3.1 6.1 1.0
CG B:HIS196 3.1 6.2 1.0
CG B:HIS69 3.1 7.5 1.0
CE1 B:HIS196 3.2 7.1 1.0
CB B:HIS196 3.3 6.3 1.0
CB B:HIS69 3.5 5.3 1.0
N2 B:LHY1309 3.7 20.1 1.0
N B:LHY1309 3.9 17.4 1.0
NH1 B:ARG127 4.1 16.0 1.0
CG B:GLU72 4.2 5.2 1.0
O B:HOH2043 4.2 13.0 1.0
O B:SER197 4.2 6.0 1.0
NE2 B:HIS69 4.2 8.1 1.0
CA B:LHY1309 4.2 16.6 1.0
CD2 B:HIS69 4.2 6.1 1.0
O B:HOH2042 4.3 7.2 1.0
CD2 B:HIS196 4.3 5.8 1.0
NE2 B:HIS196 4.3 8.6 1.0
CA B:HIS196 4.3 5.5 1.0
C B:LHY1309 4.4 15.7 1.0
OXT B:LHY1309 4.4 15.8 1.0
N B:SER197 4.6 6.2 1.0
CA B:HIS69 4.8 6.3 1.0
O2 B:LHY1309 4.9 20.2 1.0
O B:LHY1309 4.9 14.8 1.0
CZ B:ARG127 5.0 16.6 1.0
N B:HIS69 5.0 5.7 1.0

Zinc binding site 3 out of 4 in 1hee

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Zinc binding site 3 out of 4 in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1308

b:10.4
occ:1.00
 O1 D:LHY1309 2.1 19.2 1.0
OE2 D:GLU72 2.1 3.9 1.0
ND1 D:HIS69 2.1 6.0 1.0
ND1 D:HIS196 2.2 5.6 1.0
OE1 D:GLU72 2.5 8.8 1.0
CD D:GLU72 2.6 5.4 1.0
C1 D:LHY1309 3.0 20.1 1.0
CG D:HIS69 3.1 6.7 1.0
CE1 D:HIS69 3.1 7.6 1.0
CG D:HIS196 3.1 6.0 1.0
CE1 D:HIS196 3.1 6.5 1.0
CB D:HIS196 3.4 5.3 1.0
CB D:HIS69 3.4 6.3 1.0
N2 D:LHY1309 3.6 20.8 1.0
N D:LHY1309 3.9 16.7 1.0
NH1 D:ARG127 4.0 14.5 1.0
CG D:GLU72 4.1 5.6 1.0
O D:HOH2046 4.2 10.9 1.0
O D:SER197 4.2 6.7 1.0
NE2 D:HIS69 4.2 7.9 1.0
CD2 D:HIS69 4.2 6.0 1.0
NE2 D:HIS196 4.3 7.5 1.0
CD2 D:HIS196 4.3 4.8 1.0
CA D:LHY1309 4.3 15.6 1.0
O D:HOH2045 4.3 17.1 1.0
CA D:HIS196 4.4 6.1 1.0
C D:LHY1309 4.4 13.9 1.0
OXT D:LHY1309 4.4 15.0 1.0
N D:SER197 4.6 6.9 1.0
CA D:HIS69 4.8 5.1 1.0
O D:LHY1309 4.9 15.1 1.0
CZ D:ARG127 4.9 15.5 1.0
O2 D:LHY1309 4.9 23.7 1.0
N D:HIS69 5.0 6.0 1.0
CG2 D:ILE68 5.0 10.0 1.0

Zinc binding site 4 out of 4 in 1hee

Go back to Zinc Binding Sites List in 1hee
Zinc binding site 4 out of 4 in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with L-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn1308

b:9.0
occ:1.00
 O1 E:LHY1309 2.1 16.9 1.0
OE2 E:GLU72 2.1 6.7 1.0
ND1 E:HIS196 2.1 4.0 1.0
ND1 E:HIS69 2.1 8.0 1.0
OE1 E:GLU72 2.5 5.2 1.0
CD E:GLU72 2.6 5.2 1.0
C1 E:LHY1309 3.1 17.6 1.0
CE1 E:HIS196 3.1 7.1 1.0
CE1 E:HIS69 3.1 8.0 1.0
CG E:HIS69 3.1 7.0 1.0
CG E:HIS196 3.1 5.5 1.0
CB E:HIS69 3.4 6.3 1.0
CB E:HIS196 3.4 4.1 1.0
N2 E:LHY1309 3.7 18.1 1.0
N E:LHY1309 4.0 14.6 1.0
O E:HOH2045 4.1 14.2 1.0
CG E:GLU72 4.1 5.5 1.0
NH1 E:ARG127 4.1 13.2 1.0
O E:HOH2046 4.1 7.9 1.0
NE2 E:HIS196 4.2 5.6 1.0
NE2 E:HIS69 4.2 8.2 1.0
O E:SER197 4.2 6.5 1.0
CD2 E:HIS69 4.2 7.0 1.0
CD2 E:HIS196 4.2 4.4 1.0
CA E:LHY1309 4.3 14.0 1.0
C E:LHY1309 4.4 11.2 1.0
CA E:HIS196 4.4 5.5 1.0
OXT E:LHY1309 4.4 9.0 1.0
N E:SER197 4.6 7.2 1.0
CA E:HIS69 4.8 6.9 1.0
O E:LHY1309 4.8 11.6 1.0
CZ E:ARG127 4.9 13.1 1.0
N E:HIS69 5.0 5.4 1.0
CG2 E:ILE68 5.0 8.0 1.0

Reference:

J.H.Cho, D.H.Kim, S.J.Chung, N.-C.Ha, B.-H.Oh, K.Y.Choi. Insight Into the Stereochemistry in the Inhibition of Carboxypeptidase A with N- (Hydroxyaminocarbonyl)Phenylalanine: Binding Modes of An Enantiomeric Pair of the Inhibitor to Carboxypeptidase A Bioorg.Med.Chem. V. 10 2015 2002.
ISSN: ISSN 0968-0896
PubMed: 11937361
DOI: 10.1016/S0968-0896(01)00429-1
Page generated: Sun Oct 13 02:13:13 2024

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