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Copper in PDB 1ekj: The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum

Enzymatic activity of The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum

All present enzymatic activity of The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum:
4.2.1.1;

Protein crystallography data

The structure of The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum, PDB code: 1ekj was solved by M.S.Kimber, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.93
Space group C 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 136.909, 143.318, 202.135, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 25

Copper Binding Sites:

The binding sites of Copper atom in the The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum (pdb code 1ekj). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum, PDB code: 1ekj:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1ekj

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Copper binding site 1 out of 4 in the The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu4

b:73.5
occ:0.50
O B:HOH1085 2.0 44.3 1.0
SG A:CYS166 2.5 71.4 1.0
SG B:CYS166 2.7 82.0 1.0
CD B:PRO167 3.4 83.7 1.0
CG B:PRO167 3.5 83.6 1.0
NH1 B:ARG182 3.6 58.7 1.0
OG B:SER168 3.7 92.5 1.0
NH1 A:ARG182 3.8 46.8 1.0
N B:SER168 4.0 88.1 1.0
CB B:SER168 4.0 90.8 1.0
OG A:SER168 4.1 75.0 1.0
CB B:CYS166 4.1 80.5 1.0
N B:PRO167 4.1 83.0 1.0
CB A:CYS166 4.2 65.8 1.0
CD A:PRO167 4.4 70.2 1.0
CA B:CYS166 4.4 80.4 1.0
CB A:SER168 4.4 74.0 1.0
CD B:ARG182 4.5 58.5 1.0
C B:CYS166 4.5 81.4 1.0
CG A:PRO167 4.6 70.1 1.0
CZ B:ARG182 4.6 58.8 1.0
CA B:SER168 4.7 89.9 1.0
CD A:ARG182 4.7 46.9 1.0
CA A:CYS166 4.8 65.5 1.0
N A:SER168 4.8 72.4 1.0
CB B:PRO167 4.8 84.0 1.0
CA B:PRO167 4.9 84.5 1.0
CZ A:ARG182 5.0 45.3 1.0
C B:PRO167 5.0 86.2 1.0

Copper binding site 2 out of 4 in 1ekj

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Copper binding site 2 out of 4 in the The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1

b:51.9
occ:0.50
SG D:CYS166 2.4 32.0 0.5
SG C:CYS166 2.5 35.5 0.5
NH1 C:ARG182 3.5 23.9 1.0
OG C:SER168 3.6 56.8 1.0
NH1 D:ARG182 3.7 23.6 1.0
OG D:SER168 3.8 49.5 1.0
CB C:CYS166 4.1 36.5 0.5
CB D:CYS166 4.1 31.3 0.5
CB D:SER168 4.1 46.6 1.0
CB C:CYS166 4.2 40.2 0.5
CB C:SER168 4.2 52.9 1.0
CD D:PRO167 4.3 33.5 1.0
N D:SER168 4.3 42.5 1.0
CG D:PRO167 4.4 35.3 1.0
CB D:CYS166 4.4 31.4 0.5
CD C:PRO167 4.5 42.2 1.0
CD D:ARG182 4.5 23.6 1.0
N C:SER168 4.5 49.1 1.0
CD C:ARG182 4.5 27.9 1.0
CG C:PRO167 4.5 44.1 1.0
N D:PRO167 4.6 34.6 1.0
CZ C:ARG182 4.6 21.4 1.0
CA C:CYS166 4.6 39.2 0.5
CA D:CYS166 4.7 31.8 0.5
CA C:CYS166 4.7 37.0 0.5
CA D:CYS166 4.7 32.0 0.5
N C:PRO167 4.8 41.8 1.0
CZ D:ARG182 4.8 27.6 1.0
CA D:SER168 4.8 45.0 1.0
C D:CYS166 4.8 33.5 0.5
C D:CYS166 4.9 33.4 0.5
C C:CYS166 4.9 40.7 0.5
C C:CYS166 4.9 39.6 0.5

Copper binding site 3 out of 4 in 1ekj

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Copper binding site 3 out of 4 in the The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu3

b:53.4
occ:0.50
O E:HOH1302 2.0 51.4 1.0
SG F:CYS166 2.3 67.9 1.0
SG E:CYS166 2.3 63.9 1.0
NH1 F:ARG182 3.7 39.5 1.0
OG E:SER168 3.7 62.3 1.0
CB E:SER168 3.8 61.0 1.0
CB F:CYS166 3.8 62.0 1.0
OG F:SER168 3.9 65.1 1.0
NH1 E:ARG182 3.9 38.1 1.0
CB F:SER168 3.9 63.1 1.0
CB E:CYS166 4.1 54.6 1.0
N E:SER168 4.2 59.8 1.0
CD F:PRO167 4.3 59.7 1.0
N F:SER168 4.3 60.7 1.0
CD E:PRO167 4.4 56.7 1.0
CG E:PRO167 4.4 57.3 1.0
CG F:PRO167 4.4 59.2 1.0
CA F:CYS166 4.4 60.1 1.0
N F:PRO167 4.6 60.0 1.0
CA E:SER168 4.7 61.3 1.0
N E:PRO167 4.7 55.7 1.0
CA E:CYS166 4.7 53.5 1.0
C F:CYS166 4.7 60.2 1.0
CD F:ARG182 4.8 40.4 1.0
CA F:SER168 4.8 62.7 1.0
CZ F:ARG182 4.8 37.6 1.0
CD E:ARG182 4.9 39.0 1.0
C E:CYS166 4.9 54.8 1.0

Copper binding site 4 out of 4 in 1ekj

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Copper binding site 4 out of 4 in the The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of The X-Ray Crystallographic Structure of Beta Carbonic Anhydrase From the C3 Dicot Pisum Sativum within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu2

b:50.0
occ:0.50
O H:HOH1932 2.0 43.3 1.0
O G:HOH1935 2.0 40.7 1.0
OG G:SER168 2.8 52.9 1.0
SG H:CYS166 3.2 35.7 0.5
NH1 G:ARG182 3.4 28.1 1.0
CB G:SER168 3.5 49.1 1.0
CD G:PRO167 3.6 42.3 1.0
CB G:CYS166 3.7 45.8 0.5
N G:SER168 3.7 46.6 1.0
CB G:CYS166 3.7 45.2 0.5
CA G:CYS166 3.9 43.5 0.5
CA G:CYS166 3.9 43.8 0.5
CG G:PRO167 3.9 41.4 1.0
N G:PRO167 3.9 43.1 1.0
OG H:SER168 4.0 49.9 1.0
C G:CYS166 4.1 43.4 0.5
C G:CYS166 4.1 43.3 0.5
CA G:SER168 4.2 48.9 1.0
NH1 H:ARG182 4.3 24.3 1.0
SG G:CYS166 4.4 52.6 0.5
CB H:SER168 4.4 43.1 1.0
CD G:ARG182 4.5 30.3 1.0
CZ G:ARG182 4.5 28.7 1.0
CB H:CYS166 4.7 34.1 0.5
CB H:CYS166 4.7 32.7 0.5
C G:PRO167 4.7 44.9 1.0
CA G:PRO167 4.8 43.2 1.0
NE G:ARG182 4.9 27.9 1.0
O G:CYS166 5.0 43.0 0.5
O G:CYS166 5.0 42.9 0.5

Reference:

M.S.Kimber, E.F.Pai. The Active Site Architecture of Pisum Sativum Beta-Carbonic Anhydrase Is A Mirror Image of That of Alpha-Carbonic Anhydrases. Embo J. V. 19 1407 2000.
ISSN: ISSN 0261-4189
PubMed: 10747009
DOI: 10.1093/EMBOJ/19.7.1407
Page generated: Wed Sep 2 21:41:29 2020
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