Chlorine in PDB 7ocr: Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii

The structure of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocr was solved by H.K.Tam, V.Mueller, K.M.Pos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.71 / 2.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.886, 157.556, 220.467, 90, 90, 90
R / Rfree (%)	23 / 25.8

The structure of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Potassium	(K)	1 atom

The binding sites of Chlorine atom in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii (pdb code 7ocr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 7 binding sites of Chlorine where determined in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocr:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl809 b:75.5 occ:1.00 O A:HOH931 3.0 62.8 1.0 N A:VAL414 3.3 72.1 1.0 O A:VAL414 3.6 75.0 1.0 CL A:CL811 3.7 75.7 1.0 CA A:ASN374 3.7 96.0 1.0 CA A:VAL413 3.8 71.6 1.0 O A:LEU373 3.9 90.9 1.0 C A:VAL413 4.0 70.8 1.0 CB A:ASN374 4.0 96.8 1.0 N A:ASN374 4.1 94.2 1.0 CG A:ASN374 4.1 97.2 1.0 C6N A:NDP803 4.2 91.3 1.0 C A:LEU373 4.2 91.6 1.0 CA A:VAL414 4.2 72.0 1.0 OD1 A:ASN374 4.2 97.5 1.0 O A:HOH919 4.2 66.5 1.0 C5N A:NDP803 4.3 91.4 1.0 CB A:VAL414 4.3 72.4 1.0 O A:THR412 4.4 73.4 1.0 C A:VAL414 4.4 73.5 1.0 CE A:LYS527 4.4 75.5 1.0 CG1 A:VAL413 4.7 72.6 1.0 CB A:VAL413 4.7 71.8 1.0 N A:VAL413 4.7 70.6 1.0 ND2 A:ASN374 4.8 97.5 1.0 C A:THR412 4.9 71.5 1.0 CG2 A:VAL414 4.9 71.3 1.0 CD A:LYS527 4.9 74.2 1.0 CG A:LYS527 4.9 74.8 1.0 C A:ASN374 5.0 99.0 1.0 NZ A:LYS527 5.0 75.0 1.0

Chlorine binding site 2 out of 7 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl810 b:57.6 occ:1.00 OG A:SER119 2.9 65.9 1.0 N A:LYS151 3.3 65.7 1.0 CA A:GLY150 3.5 67.8 1.0 CB A:SER119 3.6 66.3 1.0 CA A:SER119 3.7 65.7 1.0 CD1 A:ILE156 3.8 60.8 1.0 CG A:LYS151 3.9 63.1 1.0 C A:GLY150 3.9 67.0 1.0 CA A:GLY144 4.1 72.6 1.0 CD A:LYS151 4.1 62.7 1.0 CB A:LYS151 4.2 64.2 1.0 CE A:LYS151 4.4 61.8 1.0 CA A:LYS151 4.4 64.9 1.0 N A:SER119 4.5 63.8 1.0 O A:THR118 4.7 62.6 1.0 CG2 A:VAL147 4.8 71.9 1.0 CG2 A:ILE156 4.8 60.1 1.0 CB A:ILE156 4.9 60.6 1.0 C A:SER119 4.9 67.0 1.0 CG1 A:ILE156 4.9 60.2 1.0 C A:THR118 4.9 62.3 1.0 N A:GLY150 4.9 69.5 1.0 N A:GLY144 4.9 71.4 1.0 O A:SER119 5.0 68.6 1.0

Chlorine binding site 3 out of 7 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl811 b:75.7 occ:1.00 O A:HOH919 2.9 66.5 1.0 OE1 A:GLN524 3.6 78.4 1.0 CL A:CL809 3.7 75.5 1.0 CG A:GLN524 3.7 77.9 1.0 OD1 A:ASN374 3.9 97.5 1.0 N A:LYS375 4.0 100.2 1.0 CD A:GLN524 4.1 78.4 1.0 O A:LYS375 4.1 101.3 1.0 O A:LEU373 4.2 90.9 1.0 CA A:ASN374 4.2 96.0 1.0 C A:ASN374 4.3 99.0 1.0 C A:LYS375 4.3 102.8 1.0 CG A:LYS527 4.4 74.8 1.0 CG2 A:VAL413 4.5 73.0 1.0 O A:THR412 4.6 73.4 1.0 CA A:LYS375 4.7 103.0 1.0 N A:VAL376 4.8 105.0 1.0 CG A:ASN374 4.8 97.2 1.0 O A:HOH931 4.9 62.8 1.0 CB A:GLN524 5.0 76.4 1.0

Chlorine binding site 4 out of 7 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl812 b:67.0 occ:1.00 N A:GLY99 3.0 54.4 1.0 N A:GLN244 3.2 55.8 1.0 NE2 A:GLN102 3.3 52.1 1.0 CA A:GLY99 3.5 53.6 1.0 CB A:GLN244 3.7 57.1 1.0 CB A:ASN243 3.7 54.1 1.0 CG A:GLN244 3.8 57.0 1.0 CA A:ASN243 4.0 54.7 1.0 CA A:GLN244 4.0 57.0 1.0 C A:LYS98 4.0 55.1 1.0 C A:ASN243 4.1 55.8 1.0 CG A:GLN102 4.1 51.2 1.0 CG A:LYS98 4.1 58.7 1.0 CE1 A:TYR216 4.2 56.1 1.0 CD A:GLN102 4.2 51.4 1.0 CA A:LYS98 4.3 56.5 1.0 C A:GLY99 4.4 52.9 1.0 CD A:GLN244 4.4 57.5 1.0 C A:GLN244 4.7 57.2 1.0 CG A:ASN243 4.8 54.8 1.0 NE2 A:GLN244 4.8 57.1 1.0 CB A:LYS98 4.8 58.0 1.0 N A:LEU100 4.8 52.9 1.0 N A:LEU245 4.9 56.3 1.0 CD1 A:TYR216 4.9 56.1 1.0 OE1 A:GLN244 5.0 58.4 1.0

Chlorine binding site 5 out of 7 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl801 b:64.2 occ:1.00 N B:GLU548 3.4 69.9 1.0 CG1 B:VAL552 3.7 68.1 1.0 N B:SER549 3.7 67.3 1.0 CB B:VAL552 3.8 66.8 1.0 CA B:TYR547 3.9 70.9 1.0 CD1 B:TYR547 4.0 70.3 1.0 CB B:SER549 4.1 65.8 1.0 C B:TYR547 4.1 70.3 1.0 CG2 B:VAL552 4.2 66.5 1.0 CA B:GLU548 4.3 69.8 1.0 CB B:TYR547 4.3 69.8 1.0 C B:GLU548 4.4 68.3 1.0 CB B:GLU548 4.5 71.2 1.0 CA B:SER549 4.5 65.8 1.0 CG B:TYR547 4.7 70.1 1.0 O B:SER549 4.7 65.4 1.0 NE2 A:GLN163 4.7 62.2 1.0 CE1 B:TYR547 4.9 70.7 1.0

Chlorine binding site 6 out of 7 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl802 b:50.0 occ:1.00 CD B:PRO611 3.6 73.3 1.0 CG B:LEU612 3.8 78.7 1.0 N B:LEU612 3.9 74.6 1.0 CB B:LEU612 3.9 77.6 1.0 CD1 B:LEU612 4.0 80.8 1.0 N B:PRO611 4.0 72.6 1.0 CA B:ASP610 4.2 73.3 1.0 CD2 B:LEU653 4.2 90.1 1.0 C B:ASP610 4.3 72.6 1.0 CG2 B:ILE655 4.4 99.0 1.0 CG B:PRO611 4.5 73.2 1.0 CA B:LEU612 4.6 75.7 1.0 CB B:PRO611 4.8 73.2 1.0 CA B:PRO611 4.8 72.3 1.0 C B:PRO611 4.9 73.1 1.0 N B:ASP610 5.0 72.6 1.0

Chlorine binding site 7 out of 7 in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:85.7 occ:1.00 N B:GLY99 3.0 89.1 1.0 NE2 B:GLN102 3.1 84.6 1.0 N B:GLN244 3.3 81.7 1.0 CA B:GLY99 3.5 88.3 1.0 CB B:ASN243 3.8 79.0 1.0 CB B:GLN244 3.8 85.1 1.0 CG B:GLN102 3.8 83.0 1.0 CG B:GLN244 3.8 85.7 1.0 CD B:GLN102 3.9 83.4 1.0 CA B:ASN243 4.0 79.3 1.0 C B:LYS98 4.0 91.2 1.0 C B:ASN243 4.1 80.2 1.0 CA B:GLN244 4.1 82.8 1.0 CG B:LYS98 4.2 90.8 1.0 C B:GLY99 4.2 88.2 1.0 CA B:LYS98 4.3 91.8 1.0 CD B:GLN244 4.4 88.2 1.0 NE2 B:GLN244 4.6 88.8 1.0 N B:LEU100 4.6 89.0 1.0 CE2 B:TYR216 4.7 89.9 1.0 CB B:GLN102 4.8 83.7 1.0 CB B:LYS98 4.8 92.6 1.0 CG B:ASN243 4.9 77.8 1.0 N B:GLN102 4.9 83.6 1.0 O B:GLY99 5.0 87.3 1.0 C B:GLN244 5.0 82.3 1.0 N B:LEU245 5.0 80.6 1.0 CD2 B:TYR216 5.0 91.8 1.0

H.K.Tam, P.Konig, S.Himpich, N.D.Ngu, R.Abele, V.Muller, K.M.Pos. Unidirectional Mannitol Synthesis of Acinetobacter Baumannii Mtld Is Facilitated By the Helix-Loop-Helix-Mediated Dimer Formation. Proc.Natl.Acad.Sci.Usa V. 119 94119 2022.
ISSN: ESSN 1091-6490
PubMed: 35363566
DOI: 10.1073/PNAS.2107994119