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Chlorine in PDB 5swc: The Structure of the Beta-Carbonic Anhydrase Ccaa

Enzymatic activity of The Structure of the Beta-Carbonic Anhydrase Ccaa

All present enzymatic activity of The Structure of the Beta-Carbonic Anhydrase Ccaa:
4.2.1.1;

Protein crystallography data

The structure of The Structure of the Beta-Carbonic Anhydrase Ccaa, PDB code: 5swc was solved by M.S.Kimber, L.Mcgurn, S.A.White, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.82 / 1.45
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 202.950, 202.950, 70.510, 90.00, 90.00, 90.00
R / Rfree (%) 13.1 / 14.7

Other elements in 5swc:

The structure of The Structure of the Beta-Carbonic Anhydrase Ccaa also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of the Beta-Carbonic Anhydrase Ccaa (pdb code 5swc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the The Structure of the Beta-Carbonic Anhydrase Ccaa, PDB code: 5swc:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in 5swc

Go back to Chlorine Binding Sites List in 5swc
Chlorine binding site 1 out of 5 in the The Structure of the Beta-Carbonic Anhydrase Ccaa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:26.1
occ:1.00
HZ3 A:LYS160 2.4 36.6 1.0
HE22 A:GLN163 2.4 27.4 1.0
H A:GLU212 2.5 23.1 1.0
O A:HOH448 2.9 27.1 1.0
O A:HOH526 3.0 32.5 1.0
HB2 A:GLU212 3.1 24.2 1.0
NZ A:LYS160 3.2 30.5 1.0
NE2 A:GLN163 3.3 22.9 1.0
HA A:LEU211 3.4 24.4 1.0
HG3 A:GLU212 3.4 23.4 1.0
N A:GLU212 3.4 19.2 1.0
HZ1 A:LYS160 3.4 36.6 1.0
HB2 A:ASP215 3.5 31.0 1.0
HD3 A:LYS160 3.6 23.6 1.0
HE2 A:LYS160 3.7 28.4 1.0
HZ2 A:LYS160 3.8 36.6 1.0
CB A:GLU212 3.8 20.2 1.0
HE21 A:GLN163 3.8 27.4 1.0
OE1 A:GLN163 3.8 22.8 1.0
CE A:LYS160 3.9 23.7 1.0
CG A:GLU212 3.9 19.4 1.0
CD A:GLN163 4.0 22.4 1.0
HD23 A:LEU211 4.1 35.3 1.0
OE1 A:GLU212 4.1 27.9 1.0
CA A:GLU212 4.2 19.8 1.0
CA A:LEU211 4.2 20.4 1.0
CD A:LYS160 4.2 19.6 1.0
C A:LEU211 4.3 18.4 1.0
CD A:GLU212 4.3 22.6 1.0
CB A:ASP215 4.3 25.9 1.0
HB3 A:ASP215 4.4 31.0 1.0
HD22 A:LEU211 4.4 35.3 1.0
O A:GLU212 4.4 21.0 1.0
O A:ALA210 4.4 19.4 1.0
O F:HOH419 4.4 31.4 1.0
HZ1 F:LYS160 4.5 34.6 0.7
HZ3 F:LYS160 4.5 34.6 0.7
HZ2 F:LYS160 4.5 34.6 0.7
O A:HOH510 4.6 21.3 1.0
OD2 A:ASP215 4.6 32.0 1.0
HB3 A:GLU212 4.6 24.2 1.0
HD2 A:LYS160 4.6 23.6 1.0
HB3 A:LEU211 4.7 23.0 1.0
CD2 A:LEU211 4.7 29.4 1.0
NZ F:LYS160 4.7 28.9 0.7
C A:GLU212 4.8 21.0 1.0
HE3 A:LYS160 4.8 28.4 1.0
HG2 A:GLU212 4.8 23.4 1.0
O A:HOH544 4.9 41.6 1.0
HA A:GLU212 5.0 23.8 1.0
CB A:LEU211 5.0 19.1 1.0

Chlorine binding site 2 out of 5 in 5swc

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Chlorine binding site 2 out of 5 in the The Structure of the Beta-Carbonic Anhydrase Ccaa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:18.1
occ:1.00
HH11 A:ARG61 2.4 15.5 1.0
HH11 B:ARG61 2.4 16.5 1.0
HD2 B:ARG61 2.9 15.1 1.0
HD2 A:ARG61 3.0 14.2 1.0
HD2 B:PRO46 3.1 21.1 1.0
HD2 A:PRO46 3.2 21.4 1.0
NH1 A:ARG61 3.2 12.9 1.0
NH1 B:ARG61 3.2 13.7 1.0
O A:HOH414 3.2 34.1 1.0
O B:HOH413 3.3 31.3 1.0
HH12 A:ARG61 3.5 15.5 1.0
HD3 B:ARG61 3.5 15.1 1.0
HD3 A:ARG61 3.5 14.2 1.0
HH12 B:ARG61 3.5 16.5 1.0
HG11 A:VAL59 3.6 16.3 1.0
HG11 B:VAL59 3.6 16.1 1.0
HG2 B:PRO46 3.6 25.8 1.0
CD B:ARG61 3.6 12.6 1.0
HG2 A:PRO46 3.7 25.5 1.0
CD A:ARG61 3.7 11.8 1.0
CD B:PRO46 3.9 17.6 1.0
CD A:PRO46 4.0 17.8 1.0
CZ A:ARG61 4.2 11.9 1.0
CZ B:ARG61 4.2 11.6 1.0
HD3 B:PRO46 4.2 21.1 1.0
HD22 B:ASN47 4.2 15.5 0.5
CG B:PRO46 4.2 21.5 1.0
HD22 A:ASN47 4.2 18.0 0.6
CG A:PRO46 4.3 21.3 1.0
HD3 A:PRO46 4.3 21.4 1.0
HG21 A:VAL59 4.3 16.4 1.0
HG21 B:VAL59 4.3 15.1 1.0
NE B:ARG61 4.3 12.3 1.0
NE A:ARG61 4.4 11.7 1.0
CG1 A:VAL59 4.5 13.6 1.0
CG1 B:VAL59 4.5 13.4 1.0
HG3 B:PRO46 4.6 25.8 1.0
HG3 A:PRO46 4.6 25.5 1.0
HA B:ASP45 4.7 20.2 1.0
HB A:VAL59 4.7 14.3 1.0
HA A:ASP45 4.7 20.5 1.0
HB B:VAL59 4.7 13.0 1.0
HG3 B:ARG61 4.8 16.0 1.0
HG3 A:ARG61 4.8 14.9 1.0
HG12 A:VAL59 4.8 16.3 1.0
HG12 B:VAL59 4.8 16.1 1.0
CG B:ARG61 4.9 13.3 1.0
ND2 B:ASN47 4.9 12.9 0.5
CG A:ARG61 4.9 12.4 1.0
HD21 A:ASN47 4.9 18.0 0.6
ND2 A:ASN47 4.9 15.0 0.6
HD21 B:ASN47 4.9 15.5 0.5

Chlorine binding site 3 out of 5 in 5swc

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Chlorine binding site 3 out of 5 in the The Structure of the Beta-Carbonic Anhydrase Ccaa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl302

b:24.3
occ:1.00
HH11 C:ARG61 2.3 23.5 1.0
HH11 D:ARG61 2.4 23.6 1.0
HD2 D:ARG61 3.0 20.7 1.0
HD2 C:ARG61 3.0 20.3 1.0
O D:HOH505 3.0 43.2 1.0
NH1 C:ARG61 3.1 19.6 1.0
NH1 D:ARG61 3.2 19.6 1.0
HD2 D:PRO46 3.2 26.0 1.0
HD2 C:PRO46 3.2 29.3 1.0
O C:HOH437 3.2 40.9 1.0
HH12 C:ARG61 3.4 23.5 1.0
HH12 D:ARG61 3.5 23.6 1.0
HD3 C:ARG61 3.5 20.3 1.0
HD3 D:ARG61 3.6 20.7 1.0
HG11 D:VAL59 3.6 22.1 1.0
CD C:ARG61 3.7 16.9 1.0
CD D:ARG61 3.7 17.2 1.0
HG11 C:VAL59 3.7 23.3 1.0
HG2 C:PRO46 3.7 32.6 1.0
HG2 D:PRO46 3.9 34.1 1.0
CD C:PRO46 4.0 24.4 1.0
CD D:PRO46 4.0 21.7 1.0
CZ C:ARG61 4.1 16.9 1.0
HD3 C:PRO46 4.2 29.3 1.0
CZ D:ARG61 4.2 18.5 1.0
HD3 D:PRO46 4.2 26.0 1.0
HG21 D:VAL59 4.3 21.5 1.0
CG C:PRO46 4.3 27.1 1.0
NE C:ARG61 4.3 14.9 1.0
HG21 C:VAL59 4.4 19.1 1.0
NE D:ARG61 4.4 15.4 1.0
HD22 C:ASN47 4.5 45.6 1.0
CG D:PRO46 4.5 28.4 1.0
CG1 D:VAL59 4.5 18.4 1.0
CG1 C:VAL59 4.6 19.4 1.0
HA D:ASP45 4.6 26.3 1.0
HB D:VAL59 4.7 19.0 1.0
HB C:VAL59 4.7 18.3 1.0
HA C:ASP45 4.7 28.9 1.0
HG3 C:PRO46 4.7 32.6 1.0
HG3 D:ARG61 4.8 19.3 1.0
HG3 C:ARG61 4.8 18.2 1.0
HG12 D:VAL59 4.8 22.1 1.0
HG12 C:VAL59 4.9 23.3 1.0
CG D:ARG61 4.9 16.1 1.0
CG C:ARG61 4.9 15.1 1.0

Chlorine binding site 4 out of 5 in 5swc

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Chlorine binding site 4 out of 5 in the The Structure of the Beta-Carbonic Anhydrase Ccaa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl302

b:26.7
occ:1.00
HZ3 E:LYS160 2.3 42.8 1.0
HE22 E:GLN163 2.4 23.4 1.0
H E:GLU212 2.5 24.5 1.0
O E:HOH474 2.8 26.7 1.0
O E:HOH459 3.1 34.6 1.0
NZ E:LYS160 3.2 35.7 1.0
HA E:LEU211 3.2 26.1 1.0
HB2 E:GLU212 3.2 25.7 1.0
NE2 E:GLN163 3.3 19.5 1.0
N E:GLU212 3.3 20.4 1.0
HZ1 E:LYS160 3.4 42.8 1.0
HG3 E:GLU212 3.5 27.4 1.0
HB2 E:ASP215 3.6 37.7 1.0
HD3 E:LYS160 3.6 22.6 1.0
HE2 E:LYS160 3.7 36.6 1.0
HZ2 E:LYS160 3.7 42.8 1.0
HE21 E:GLN163 3.8 23.4 1.0
CE E:LYS160 3.9 30.5 1.0
CB E:GLU212 3.9 21.4 1.0
OE1 E:GLN163 3.9 22.1 1.0
HD23 E:LEU211 4.0 49.5 1.0
HD22 E:LEU211 4.0 49.5 1.0
CA E:LEU211 4.0 21.7 1.0
CD E:GLN163 4.0 20.0 1.0
CG E:GLU212 4.1 22.8 1.0
C E:LEU211 4.2 19.7 1.0
CA E:GLU212 4.2 21.1 1.0
OE1 E:GLU212 4.2 29.4 1.0
CD E:LYS160 4.2 18.8 1.0
O E:HOH496 4.4 21.5 1.0
O E:GLU212 4.4 23.5 1.0
HB3 E:LEU211 4.4 28.5 1.0
HB3 E:ASP215 4.4 37.7 1.0
CB E:ASP215 4.4 31.4 1.0
CD E:GLU212 4.4 30.1 1.0
CD2 E:LEU211 4.4 41.2 1.0
O E:ALA210 4.5 18.6 1.0
O E:HOH417 4.6 42.0 1.0
OD2 E:ASP215 4.6 34.0 1.0
HD2 E:LYS160 4.7 22.6 1.0
CB E:LEU211 4.7 23.7 1.0
HB3 E:GLU212 4.7 25.7 1.0
O D:HOH508 4.7 31.1 1.0
HE3 E:LYS160 4.8 36.6 1.0
C E:GLU212 4.8 22.6 1.0
HG2 E:GLU212 5.0 27.4 1.0
HB3 E:LEU159 5.0 20.0 1.0

Chlorine binding site 5 out of 5 in 5swc

Go back to Chlorine Binding Sites List in 5swc
Chlorine binding site 5 out of 5 in the The Structure of the Beta-Carbonic Anhydrase Ccaa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of The Structure of the Beta-Carbonic Anhydrase Ccaa within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl303

b:25.1
occ:1.00
HH11 E:ARG61 2.3 21.5 1.0
HH11 F:ARG61 2.3 20.1 1.0
HD2 E:ARG61 2.9 19.3 1.0
HD2 F:ARG61 3.0 17.6 1.0
NH1 E:ARG61 3.1 17.9 1.0
NH1 F:ARG61 3.1 16.8 1.0
HD2 E:PRO46 3.2 22.8 1.0
HD2 F:PRO46 3.2 30.6 1.0
O E:HOH430 3.3 39.4 1.0
HH12 E:ARG61 3.4 21.5 1.0
HH12 F:ARG61 3.4 20.1 1.0
HD3 F:ARG61 3.5 17.6 1.0
HD3 E:ARG61 3.5 19.3 1.0
HG11 E:VAL59 3.6 19.1 1.0
CD E:ARG61 3.6 16.1 1.0
HG11 F:VAL59 3.6 19.8 1.0
CD F:ARG61 3.7 14.7 1.0
HG2 E:PRO46 3.7 28.4 1.0
HG2 F:PRO46 3.8 31.3 1.0
CD E:PRO46 4.0 19.0 1.0
CD F:PRO46 4.0 25.5 1.0
CZ E:ARG61 4.1 16.1 1.0
CZ F:ARG61 4.1 16.8 1.0
HD3 E:PRO46 4.2 22.8 1.0
HD3 F:PRO46 4.2 30.6 1.0
NE E:ARG61 4.3 15.2 1.0
CG E:PRO46 4.3 23.7 1.0
HG21 F:VAL59 4.3 21.5 1.0
NE F:ARG61 4.3 15.5 1.0
HG21 E:VAL59 4.4 17.9 1.0
CG F:PRO46 4.4 26.1 1.0
CG1 E:VAL59 4.5 15.9 1.0
CG1 F:VAL59 4.5 16.5 1.0
HB F:VAL59 4.6 17.9 1.0
HA E:ASP45 4.7 21.4 1.0
HA F:ASP45 4.7 25.6 1.0
HB E:VAL59 4.7 15.7 1.0
HG3 E:ARG61 4.7 17.2 1.0
HG3 F:ARG61 4.8 17.6 1.0
HG12 E:VAL59 4.8 19.1 1.0
HG12 F:VAL59 4.8 19.8 1.0
HG3 E:PRO46 4.8 28.4 1.0
CG E:ARG61 4.8 14.4 1.0
CG F:ARG61 4.9 14.7 1.0

Reference:

L.D.Mcgurn, M.Moazami-Goudarzi, S.A.White, T.Suwal, B.Brar, J.Q.Tang, G.S.Espie, M.S.Kimber. The Structure, Kinetics and Interactions of the Beta-Carboxysomal Beta-Carbonic Anhydrase, Ccaa. Biochem. J. V. 473 4559 2016.
ISSN: ESSN 1470-8728
PubMed: 27729545
DOI: 10.1042/BCJ20160773
Page generated: Sat Jul 12 08:39:12 2025

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