Iodine in PDB 3uco: Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide

All present enzymatic activity of Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide:
4.2.1.1;

The structure of Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide, PDB code: 3uco was solved by S.Huang, T.Hainzl, A.E.Sauer-Eriksson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.94 / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.478, 75.478, 222.405, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 21.1

The structure of Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iodine atom in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide (pdb code 3uco). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 3 binding sites of Iodine where determined in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide, PDB code: 3uco:
Jump to Iodine binding site number: 1; 2; 3;

Iodine binding site 1 out of 3 in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide within 5.0Å range: probe atom residue distance (Å) B Occ A:I229 b:69.5 occ:1.00 O A:HOH231 2.2 26.7 1.0 CE2 B:TYR88 3.7 58.0 1.0 ZN A:ZN228 3.8 51.5 1.0 N A:ALA108 4.0 49.6 1.0 CZ B:PHE66 4.1 51.8 1.0 SG A:CYS47 4.1 48.9 1.0 CG1 A:VAL71 4.1 35.6 1.0 CE1 B:PHE66 4.1 51.4 1.0 N A:GLY107 4.2 48.7 1.0 CD2 B:TYR88 4.3 53.0 1.0 CZ B:TYR88 4.3 61.1 1.0 CA A:GLY107 4.3 48.9 1.0 CB A:ALA108 4.4 49.6 1.0 OH B:TYR88 4.5 60.6 1.0 C A:GLY107 4.5 50.2 1.0 NE2 B:GLN38 4.6 61.4 1.0 CG2 A:VAL71 4.7 33.9 1.0 OD2 A:ASP49 4.7 48.1 1.0 CA A:ALA108 4.7 50.1 1.0 CB A:VAL71 4.8 37.0 1.0 SG A:CYS106 4.9 49.3 1.0 CA A:VAL71 4.9 38.0 1.0

Iodine binding site 2 out of 3 in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide within 5.0Å range: probe atom residue distance (Å) B Occ A:I230 b:64.0 occ:1.00 NH1 A:ARG69 3.5 43.6 1.0 NH1 B:ARG69 3.6 46.5 1.0 CD B:PRO54 3.7 49.8 1.0 CB A:SER53 3.9 55.3 1.0 CD A:PRO54 4.0 56.5 1.0 CB B:SER53 4.2 50.3 1.0 CA A:SER53 4.2 55.8 1.0 CA B:SER53 4.3 49.7 1.0 N B:PRO54 4.3 50.5 1.0 CG A:PRO54 4.4 58.3 1.0 CG B:PRO54 4.4 50.5 1.0 N A:PRO54 4.4 56.5 1.0 CB A:ALA55 4.5 58.5 1.0 C B:SER53 4.5 49.9 1.0 N A:ALA55 4.5 57.9 1.0 N B:ALA55 4.5 52.9 1.0 C A:SER53 4.5 56.3 1.0 OG A:SER53 4.8 64.4 1.0 CB B:ALA55 4.8 52.6 1.0 CZ A:ARG69 4.8 47.9 1.0 OG B:SER53 4.8 55.6 1.0 CZ B:ARG69 4.9 50.8 1.0 CD A:ARG69 5.0 37.6 1.0

Iodine binding site 3 out of 3 in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 3 of Coccomyxa Beta-Carbonic Anhydrase in Complex with Iodide within 5.0Å range: probe atom residue distance (Å) B Occ B:I229 b:66.7 occ:1.00 O B:HOH230 2.1 35.0 1.0 ZN B:ZN228 3.9 51.0 1.0 SG B:CYS47 4.0 43.1 1.0 CE2 A:TYR88 4.0 51.8 1.0 N B:ALA108 4.0 47.5 1.0 CG1 B:VAL71 4.2 34.0 1.0 CZ A:PHE66 4.2 42.0 1.0 N B:GLY107 4.3 45.9 1.0 CE1 A:PHE66 4.3 43.2 1.0 CD2 A:TYR88 4.4 47.6 1.0 CA B:GLY107 4.4 46.1 1.0 CZ A:TYR88 4.5 54.3 1.0 CB B:ALA108 4.6 47.9 1.0 C B:GLY107 4.6 48.1 1.0 CG2 B:VAL71 4.7 34.2 1.0 NE2 A:GLN38 4.7 56.1 1.0 CB B:VAL71 4.7 38.2 1.0 OH A:TYR88 4.7 60.2 1.0 CA B:VAL71 4.8 37.2 1.0 CA B:ALA108 4.8 47.5 1.0 OD2 B:ASP49 4.8 47.5 1.0 SG B:CYS106 4.9 44.4 1.0 N B:GLY72 4.9 37.8 1.0 CB B:ASP49 5.0 46.4 1.0

S.Huang, T.Hainzl, C.Grundstrom, C.Forsman, G.Samuelsson, A.E.Sauer-Eriksson. Structural Studies of [Beta]-Carbonic Anhydrase From the Green Alga Coccomyxa: Inhibitor Complexes with Anions and Acetazolamide. Plos One V. 6 28458 2011.
ISSN: ESSN 1932-6203
PubMed: 22162771
DOI: 10.1371/JOURNAL.PONE.0028458