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Calcium in PDB 1szo: Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid

Protein crystallography data

The structure of Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid, PDB code: 1szo was solved by P.M.Leonard, G.Grogan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 83.280, 132.008, 135.424, 90.00, 94.11, 90.00
R / Rfree (%) 16.4 / 19.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid (pdb code 1szo). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid, PDB code: 1szo:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1szo

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Calcium binding site 1 out of 4 in the Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca2001

b:27.7
occ:1.00
O C:HOH5077 2.1 18.8 1.0
O B:HOH5108 2.1 18.6 1.0
O A:HOH5059 2.1 20.0 1.0
O A:HOH5058 2.4 25.5 1.0
O B:HOH5092 2.4 29.7 1.0
O C:HOH5039 2.6 24.0 1.0
O B:ASP186 3.7 13.4 1.0
O A:ASP186 3.8 14.3 1.0
O C:ASP186 3.9 13.9 1.0
NH1 A:ARG168 3.9 12.9 1.0
O B:HOH5079 3.9 22.2 1.0
O A:HOH5078 4.0 21.3 1.0
NH1 B:ARG168 4.0 12.2 1.0
NH1 C:ARG168 4.0 12.5 1.0
O C:HOH5083 4.1 26.2 1.0
O A:HOH5123 4.5 24.6 1.0
OD1 B:ASP186 4.8 25.4 1.0
CZ A:ARG168 4.8 14.1 1.0
NH2 A:ARG168 4.9 13.0 1.0
C B:ASP186 4.9 15.5 1.0
CZ B:ARG168 4.9 16.3 1.0
NH2 B:ARG168 4.9 16.8 1.0
OD1 C:ASP186 4.9 23.2 1.0
CZ C:ARG168 5.0 15.2 1.0

Calcium binding site 2 out of 4 in 1szo

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Calcium binding site 2 out of 4 in the Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Ca2002

b:37.0
occ:1.00
O E:HOH5022 2.1 21.9 1.0
O F:HOH5112 2.2 28.6 1.0
O F:HOH5132 2.5 27.4 1.0
O D:HOH5090 2.5 25.7 1.0
O E:HOH5152 2.8 30.7 1.0
O E:HOH5074 2.8 25.6 1.0
O F:ASP186 3.6 14.3 1.0
O E:ASP186 3.7 14.9 1.0
NH1 F:ARG168 3.8 14.6 1.0
O F:HOH5089 3.9 28.5 1.0
NH1 D:ARG168 4.0 15.1 1.0
NH1 E:ARG168 4.0 15.4 1.0
O D:HOH5077 4.1 29.9 1.0
O D:ASP186 4.1 14.4 1.0
O E:HOH5051 4.1 23.9 1.0
O E:HOH5131 4.4 27.9 1.0
OD1 F:ASP186 4.6 23.8 1.0
NH2 F:ARG168 4.7 17.6 1.0
CZ F:ARG168 4.7 17.8 1.0
C F:ASP186 4.8 15.8 1.0
C E:ASP186 4.9 16.1 1.0
OD1 E:ASP186 4.9 29.9 1.0
O F:HOH5037 5.0 18.4 1.0
CZ D:ARG168 5.0 15.6 1.0

Calcium binding site 3 out of 4 in 1szo

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Calcium binding site 3 out of 4 in the Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Ca2003

b:33.9
occ:1.00
O G:HOH5045 2.1 25.4 1.0
O I:HOH5057 2.1 22.2 1.0
O H:HOH5116 2.2 26.4 1.0
O I:HOH5066 2.6 30.8 1.0
O G:HOH5129 2.7 30.4 1.0
O I:HOH5069 2.7 25.5 1.0
O I:ASP186 3.7 14.7 1.0
O G:ASP186 3.9 15.0 1.0
NH1 I:ARG168 3.9 15.2 1.0
O H:HOH5112 3.9 29.4 1.0
NH1 H:ARG168 3.9 14.4 1.0
O H:ASP186 3.9 14.7 1.0
O I:HOH5089 3.9 25.8 1.0
O G:HOH5064 3.9 24.4 1.0
NH1 G:ARG168 4.0 14.3 1.0
O G:HOH5145 4.5 23.8 1.0
CZ I:ARG168 4.8 17.7 1.0
CZ H:ARG168 4.8 16.3 1.0
NH2 I:ARG168 4.8 18.7 1.0
C I:ASP186 4.9 15.4 1.0
OD1 H:ASP186 4.9 27.7 1.0
NH2 H:ARG168 4.9 20.1 1.0
OD1 I:ASP186 5.0 26.8 1.0

Calcium binding site 4 out of 4 in 1szo

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Calcium binding site 4 out of 4 in the Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase HIS122ALA Mutant Bound to Its Natural Product (2S,4S)- Alpha-Campholinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Ca2004

b:33.2
occ:1.00
O K:HOH5065 2.1 22.8 1.0
O J:HOH5111 2.2 28.7 1.0
O L:HOH5143 2.2 31.6 1.0
O J:HOH5051 2.3 22.2 1.0
O J:HOH5102 2.6 39.6 1.0
O K:HOH5066 3.0 28.0 1.0
O K:ASP186 3.7 15.5 1.0
NH1 L:ARG168 3.9 16.0 1.0
O J:ASP186 3.9 15.8 1.0
O L:ASP186 3.9 14.2 1.0
NH1 K:ARG168 4.0 17.2 1.0
O L:HOH5076 4.0 29.2 1.0
O J:HOH5088 4.0 27.4 1.0
NH1 J:ARG168 4.0 17.3 1.0
O L:HOH5115 4.1 33.0 1.0
CZ L:ARG168 4.8 17.8 1.0
OD1 K:ASP186 4.8 29.7 1.0
NH2 L:ARG168 4.8 18.6 1.0
OD1 L:ASP186 4.8 21.6 1.0
C K:ASP186 4.9 15.9 1.0
CZ K:ARG168 4.9 17.9 1.0
NH2 K:ARG168 4.9 20.0 1.0
CZ J:ARG168 5.0 17.0 1.0

Reference:

P.M.Leonard, G.Grogan. Structure of 6-Oxo Camphor Hydrolase H122A Mutant Bound to Its Natural Product, (2S,4S)-Alpha-Campholinic Acid: Mutant Structure Suggests An Atypical Mode of Transition State Binding For A Crotonase Homolog. J.Biol.Chem. V. 279 31312 2004.
ISSN: ISSN 0021-9258
PubMed: 15138275
DOI: 10.1074/JBC.M403514200
Page generated: Sat Dec 12 03:20:28 2020

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