Chlorine in PDB 4bgu: 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii

All present enzymatic activity of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii:
1.1.1.37;

The structure of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii, PDB code: 4bgu was solved by R.Talon, D.Madern, E.Girard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.479 / 1.49
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	143.760, 82.319, 112.750, 90.00, 101.72, 90.00
R / Rfree (%)	15.58 / 17.88

The structure of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii also contains other interesting chemical elements:

Potassium

(K)

23 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 50; Page 6, Binding sites: 51 - 60; Page 7, Binding sites: 61 - 70; Page 8, Binding sites: 71 - 71;

Binding sites:

The binding sites of Chlorine atom in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii (pdb code 4bgu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 71 binding sites of Chlorine where determined in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii, PDB code: 4bgu:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1313 b:17.1 occ:0.53 O A:HOH2290 2.9 37.3 1.0 O A:HOH2293 3.0 14.9 1.0 O A:HOH2387 3.0 17.7 1.0 O A:HOH2299 3.7 36.8 1.0 CG2 A:VAL156 3.9 10.4 1.0 CB A:GLN159 4.1 11.9 1.0 CA A:VAL156 4.2 10.1 1.0 CG1 A:VAL156 4.3 10.3 1.0 O A:HOH2390 4.3 35.9 1.0 CB A:VAL156 4.3 10.0 1.0 CG A:GLN159 4.4 11.9 1.0 CE2 A:TYR155 4.4 8.9 1.0 CB A:ASP207 4.4 15.1 1.0 O A:HOH2388 4.4 24.4 1.0 O A:VAL156 4.5 10.5 1.0 O A:HOH2111 4.7 20.4 1.0 O A:HOH2110 4.8 35.4 1.0 O A:ASP207 4.8 13.6 1.0 C A:VAL156 4.9 10.2 1.0 CD2 A:TYR155 5.0 8.7 1.0 CG A:ASP207 5.0 15.6 1.0 CZ A:TYR155 5.0 8.9 1.0 O A:HOH2394 5.0 26.4 1.0

Chlorine binding site 2 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1314 b:26.1 occ:0.19 O A:HOH2239 2.3 21.9 1.0 O A:HOH2084 2.7 23.4 1.0 CG2 A:VAL13 3.4 11.2 1.0 CG1 A:VAL13 3.9 10.7 1.0 O A:HOH2333 3.9 21.3 1.0 OD1 A:ASN121 4.1 16.8 0.6 CB A:VAL13 4.1 11.0 1.0 OG1 A:THR222 4.2 13.8 0.3 CB A:THR119 4.2 9.5 1.0 OG1 A:THR119 4.3 9.5 1.0 O A:HOH2238 4.3 13.8 1.0 CB A:PRO226 4.3 8.6 1.0 CG A:PRO226 4.3 9.1 1.0 O A:THR119 4.5 12.4 1.0 O A:HOH2163 4.6 26.8 1.0 ND2 A:ASN121 4.6 17.4 0.6 O A:HOH2240 4.7 26.0 1.0 CG A:ASN121 4.8 17.3 0.6

Chlorine binding site 3 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1315 b:31.6 occ:0.40 O D:HOH2269 2.6 23.8 1.0 O A:HOH2357 2.9 15.5 1.0 O D:HOH2353 3.3 23.3 1.0 CA A:GLY191 3.5 9.5 1.0 CZ2 D:TRP279 3.6 8.0 1.0 O D:HOH2242 3.8 36.5 1.0 N A:GLY191 3.9 9.1 1.0 O D:VAL244 4.0 8.5 1.0 CG1 D:VAL244 4.2 9.8 1.0 CB D:VAL244 4.2 10.2 1.0 CH2 D:TRP279 4.2 7.9 1.0 O A:HOH2358 4.3 13.9 1.0 C A:ASP190 4.3 9.9 1.0 O A:ASP190 4.3 10.8 1.0 O A:HOH2322 4.4 9.6 1.0 O A:HOH2329 4.5 20.9 1.0 O D:HOH2241 4.6 14.0 1.0 CE2 D:TRP279 4.7 8.8 1.0 O A:HOH2508 4.7 18.4 1.0 O A:HOH2324 4.7 11.5 1.0 C D:VAL244 4.7 8.9 1.0 OD1 D:ASP169 4.8 10.8 0.6 O D:HOH2352 4.8 25.6 1.0 C A:GLY191 4.9 9.3 1.0

Chlorine binding site 4 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1316 b:30.0 occ:0.74 NZ A:LYS37 3.1 29.5 1.0 N A:LYS37 3.3 25.8 1.0 CD A:PRO36 3.6 20.0 1.0 CB A:LYS37 3.6 27.7 1.0 N A:PRO36 3.7 19.2 1.0 CG A:LYS37 3.7 27.0 1.0 CE A:LYS37 3.8 29.9 1.0 CB A:ILE35 3.8 17.2 1.0 CD1 A:ILE35 3.9 18.6 1.0 O A:HOH2069 3.9 44.9 1.0 CB A:PRO36 4.0 21.3 1.0 CA A:LYS37 4.1 26.5 1.0 CG1 A:ILE35 4.1 17.3 1.0 C A:PRO36 4.2 20.2 1.0 CA A:PRO36 4.2 19.9 1.0 CG A:PRO36 4.2 20.9 1.0 C A:ILE35 4.3 16.8 1.0 CD A:LYS37 4.3 28.4 1.0 CA A:ILE35 4.6 16.2 1.0 CG2 A:ILE35 4.9 17.0 1.0

Chlorine binding site 5 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1317 b:18.5 occ:0.43 O A:HOH2189 2.6 34.8 1.0 ND2 A:ASN121 2.8 17.4 0.6 N A:VAL123 3.1 10.9 1.0 CD2 A:HIS176 3.4 12.1 1.0 CB A:ASN121 3.5 17.6 0.4 CA A:PRO122 3.5 14.2 1.0 CB A:ASN121 3.5 17.6 0.6 CG A:ASN121 3.6 17.3 0.6 CA A:ASN121 3.7 17.0 0.4 CA A:ASN121 3.7 16.9 0.6 CG1 A:VAL123 3.7 11.8 1.0 O A:HOH2190 3.7 13.1 1.0 C A:PRO122 3.8 13.5 1.0 O A:HIS176 3.8 11.5 1.0 NH2 A:ARG89 3.9 27.0 1.0 CB A:VAL123 3.9 11.1 1.0 CA A:VAL123 4.1 10.2 1.0 NH1 A:ARG89 4.1 27.6 1.0 NE2 A:HIS176 4.3 11.9 1.0 CG A:HIS176 4.3 11.7 1.0 ND2 A:ASN121 4.4 18.6 0.4 N A:PRO122 4.4 13.8 1.0 O A:HOH2332 4.4 34.3 1.0 CZ A:ARG89 4.5 27.4 1.0 CG A:ASN121 4.5 18.0 0.4 CB A:PRO122 4.5 14.1 1.0 C A:ASN121 4.6 16.7 1.0 O A:HOH2238 4.6 13.8 1.0 CB A:HIS176 4.6 11.4 1.0 N A:ASN121 4.7 16.0 1.0 OD1 A:ASN121 4.8 16.8 0.6 C A:HIS176 4.9 11.0 1.0 O A:SER120 5.0 12.1 1.0 O A:PRO122 5.0 12.3 1.0

Chlorine binding site 6 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1318 b:22.1 occ:0.32 CD A:ARG89 3.3 27.5 1.0 NZ A:LYS295 3.3 17.4 1.0 NE2 A:GLN299 3.3 17.7 1.0 CE A:LYS295 3.4 17.0 1.0 O A:HOH2186 3.6 17.7 1.0 CB A:ARG89 3.8 29.0 1.0 NE A:ARG89 3.8 27.1 1.0 CG A:ARG89 3.8 26.8 1.0 CD A:GLN299 4.4 16.3 1.0 O A:HOH2187 4.5 15.4 1.0 OE2 A:GLU175 4.6 11.8 1.0 OE1 A:GLN299 4.6 15.0 1.0 O A:HOH2180 4.7 35.1 1.0 O A:HOH2172 4.9 35.2 1.0 OD2 A:ASP178 4.9 18.4 0.5 CD A:LYS295 4.9 15.9 1.0 O A:HOH2501 4.9 27.7 1.0

Chlorine binding site 7 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1319 b:31.4 occ:0.41 NH1 A:ARG89 3.1 27.6 1.0 CD A:ARG89 3.5 27.5 1.0 ND2 A:ASN121 3.5 18.6 0.4 CG A:ARG89 3.7 26.8 1.0 CD A:ARG83 3.9 43.1 1.0 CA A:ARG89 3.9 29.4 1.0 CB A:ARG89 4.0 29.0 1.0 CD2 A:LEU92 4.1 22.3 1.0 CZ A:ARG89 4.1 27.4 1.0 NH1 A:ARG83 4.1 46.5 1.0 NE A:ARG89 4.2 27.1 1.0 O A:HOH2172 4.4 35.2 1.0 N A:ARG89 4.7 31.9 1.0 CG A:PRO122 4.7 14.9 1.0 CG A:ARG83 4.7 42.9 1.0 NE A:ARG83 4.8 45.4 1.0 O A:HOH2188 4.8 41.8 1.0 CZ A:ARG83 4.8 46.9 1.0 CG A:ASN121 4.8 18.0 0.4 CB A:ARG83 4.9 40.7 1.0

Chlorine binding site 8 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1320 b:24.2 occ:0.51 O A:HOH2306 2.9 43.3 1.0 O A:HOH2368 3.0 29.2 1.0 NE A:ARG160 3.1 12.4 1.0 NH2 A:ARG160 3.5 13.8 1.0 CD A:GLU200 3.7 22.1 1.0 CZ A:ARG160 3.8 13.0 1.0 CG A:GLU200 3.8 21.3 1.0 OE2 A:GLU200 3.8 22.6 1.0 CD1 A:PHE196 4.0 15.7 1.0 CE1 A:PHE196 4.0 15.3 1.0 OE1 A:GLU200 4.1 21.8 1.0 CD A:ARG160 4.1 12.1 1.0 CB A:GLU200 4.1 20.3 1.0 CD1 A:ILE204 4.5 13.3 1.0 CZ A:PHE161 4.5 11.9 1.0 O A:HOH2147 4.6 44.5 1.0 CE1 A:PHE161 4.9 11.4 1.0 CG A:ARG160 4.9 12.4 1.0

Chlorine binding site 9 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1321 b:24.2 occ:0.54 O A:HOH2333 3.1 21.3 1.0 NH2 A:ARG152 3.1 10.4 1.0 CG2 A:THR222 3.1 14.0 0.3 NH1 A:ARG152 3.3 10.3 1.0 OG1 A:THR222 3.4 14.1 0.7 CZ A:ARG152 3.6 10.2 1.0 CG2 A:THR222 3.7 13.9 0.7 CD1 A:ILE216 3.9 13.2 1.0 CD2 A:LEU148 4.0 9.2 1.0 CG1 A:ILE216 4.0 13.5 1.0 CB A:THR222 4.0 14.0 0.7 CB A:THR222 4.1 14.0 0.3 OG1 A:THR222 4.3 13.8 0.3 NE2 A:HIS176 4.9 11.9 1.0 NE A:ARG152 4.9 9.9 1.0

Chlorine binding site 10 out of 71 in the 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of 1.50 A Resolution Structure of the Malate Dehydrogenase From Haloferax Volcanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1322 b:17.7 occ:0.32 O A:HOH2361 2.5 39.5 1.0 O A:HOH2355 3.0 26.4 1.0 CB A:ASN192 3.2 11.2 0.5 OD1 A:ASN192 3.2 11.3 0.5 ND2 A:ASN192 3.5 11.6 0.5 CG A:ASN192 3.6 11.7 0.5 CB A:PRO194 3.7 12.7 1.0 CB A:ASN192 3.7 11.4 0.5 CG A:ASN192 3.9 11.5 0.5 CA A:PRO194 4.0 13.0 1.0 CD A:PRO194 4.1 12.6 1.0 N A:PRO194 4.2 13.0 1.0 CG A:PRO194 4.3 12.2 1.0 CE2 A:PHE161 4.4 12.3 1.0 OD1 A:ASN192 4.4 12.0 0.5 O A:HOH2147 4.6 44.5 1.0 CA A:ASN192 4.6 11.3 0.5 O A:HOH2359 4.7 22.1 1.0 C A:ASN192 4.7 10.8 1.0 O A:HOH2366 4.8 29.0 1.0 C A:ASP193 4.8 12.2 1.0 CA A:ASN192 4.8 11.4 0.5 O A:VAL189 4.8 9.4 1.0 N A:ASP193 4.9 12.8 1.0

R.Talon, E.Girard, B.Franzetti, G.Zaccai, D.Madern. Insight Into Structural Evolution of Extremophilic Proteins To Be Published.