Chlorine in PDB 7ocq: Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii

The structure of Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocq 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)	48.42 / 2.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.301, 157.337, 219.02, 90, 90, 90
R / Rfree (%)	23.2 / 28.8

The structure of Nadh 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

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

Chlorine binding site 1 out of 7 in the Nadh 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 Nadh 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:Cl807 b:85.8 occ:1.00 NH2 A:ARG613 3.1 116.0 1.0 NH1 A:ARG620 3.8 107.1 1.0 NH2 A:ARG620 4.1 107.6 1.0 CZ A:ARG613 4.3 118.5 1.0 CZ A:ARG620 4.4 107.7 1.0 CD A:LYS375 4.5 113.8 1.0 CE A:LYS614 4.6 115.3 1.0 O A:ASN374 4.9 107.8 1.0

Chlorine binding site 2 out of 7 in the Nadh 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 Nadh 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:Cl808 b:87.5 occ:1.00 O A:HOH906 3.0 67.3 1.0 N A:VAL414 3.1 87.0 1.0 O A:VAL414 3.5 90.1 1.0 CA A:ASN374 3.6 102.9 1.0 CA A:VAL413 3.8 86.4 1.0 O A:LEU373 3.8 98.9 1.0 CB A:ASN374 3.8 103.6 1.0 OD1 A:ASN374 3.8 104.0 1.0 C A:VAL413 3.9 85.6 1.0 CA A:VAL414 4.0 86.9 1.0 CG A:ASN374 4.0 104.0 1.0 C6N A:V8H801 4.0 94.4 0.7 N A:ASN374 4.0 101.8 1.0 CB A:VAL414 4.1 87.3 1.0 C A:LEU373 4.1 99.7 1.0 O A:HOH925 4.1 46.3 1.0 C5N A:V8H801 4.2 93.6 0.7 C A:VAL414 4.2 88.5 1.0 CE A:LYS527 4.4 93.6 1.0 O A:THR412 4.4 88.0 1.0 O A:HOH914 4.5 72.2 1.0 CG1 A:VAL413 4.6 87.8 1.0 CG2 A:VAL414 4.6 86.2 1.0 CB A:VAL413 4.7 86.8 1.0 N A:VAL413 4.7 85.2 1.0 ND2 A:ASN374 4.8 104.8 1.0 NZ A:LYS527 4.8 93.0 1.0 C A:THR412 4.9 86.1 1.0 O A:HOH901 4.9 68.3 1.0 C A:ASN374 4.9 105.5 1.0 CD A:LYS527 5.0 92.3 1.0

Chlorine binding site 3 out of 7 in the Nadh 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 Nadh 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:79.5 occ:1.00 N A:GLY99 3.1 68.0 1.0 N A:GLN244 3.2 70.2 1.0 CA A:GLY99 3.5 67.1 1.0 NE2 A:GLN102 3.6 66.2 1.0 CB A:ASN243 3.6 69.0 1.0 CA A:ASN243 3.8 69.5 1.0 CG A:GLN244 3.8 70.0 1.0 CB A:GLN244 3.8 70.7 1.0 CG A:GLN102 3.8 65.6 1.0 C A:ASN243 3.9 70.6 1.0 CA A:GLN244 4.1 71.0 1.0 C A:LYS98 4.1 69.0 1.0 CD A:GLN102 4.2 65.7 1.0 C A:GLY99 4.3 66.4 1.0 CD A:GLN244 4.3 69.8 1.0 CA A:LYS98 4.4 70.6 1.0 CG A:LYS98 4.5 72.5 1.0 NE2 A:GLN244 4.6 69.1 1.0 CE1 A:TYR216 4.6 71.4 1.0 N A:LEU100 4.7 66.6 1.0 CB A:GLN102 4.8 64.8 1.0 CG A:ASN243 4.9 69.7 1.0 N A:GLN102 4.9 64.7 1.0 C A:GLN244 4.9 71.5 1.0 O A:GLY99 4.9 65.6 1.0 OE1 A:GLN244 5.0 70.4 1.0

Chlorine binding site 4 out of 7 in the Nadh 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 Nadh 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:93.9 occ:1.00 CB A:LEU612 3.4 137.3 1.0 CD2 A:LEU653 3.5 139.6 1.0 CD A:PRO611 3.7 132.9 1.0 N A:LEU612 3.9 133.0 1.0 CA A:ASP610 3.9 130.3 1.0 N A:PRO611 4.2 130.2 1.0 CG A:PRO611 4.3 134.6 1.0 CA A:LEU612 4.3 134.3 1.0 CD2 A:LEU612 4.3 141.9 1.0 C A:ASP610 4.3 128.9 1.0 OD1 A:ASP610 4.4 132.2 1.0 CG A:LEU612 4.5 139.7 1.0 N A:ASP610 4.7 130.4 1.0 CB A:ASP610 4.8 128.4 1.0 CG A:LEU653 4.9 141.9 1.0 CD1 A:ILE655 4.9 149.8 1.0 C A:PRO611 5.0 130.7 1.0

Chlorine binding site 5 out of 7 in the Nadh 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 Nadh 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:Cl808 b:81.4 occ:1.00 NE B:ARG431 3.4 96.3 1.0 NH1 B:ARG431 3.4 94.2 1.0 CG B:ARG428 3.7 90.0 1.0 O1 A:GOL806 3.8 106.3 1.0 CZ B:ARG431 3.8 95.6 1.0 CB B:ARG428 3.9 89.7 1.0 C1 A:GOL806 4.0 106.8 1.0 CA B:ARG428 4.0 90.4 1.0 CE2 B:TYR427 4.1 97.5 1.0 CD2 B:TYR427 4.2 95.8 1.0 CD B:ARG431 4.5 97.8 1.0 N B:ARG428 4.6 90.8 1.0 O B:GLN424 5.0 93.0 1.0 C2 A:GOL806 5.0 107.4 1.0

Chlorine binding site 6 out of 7 in the Nadh 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 Nadh 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:Cl809 b:75.8 occ:1.00 CD B:PRO611 3.6 92.5 1.0 CG B:LEU612 3.7 98.7 1.0 CD1 B:LEU612 3.7 100.7 1.0 CB B:LEU612 4.0 97.7 1.0 CD2 B:LEU653 4.0 99.5 1.0 N B:LEU612 4.1 94.5 1.0 N B:PRO611 4.2 91.9 1.0 CG2 B:ILE655 4.3 105.1 1.0 CA B:ASP610 4.3 93.0 1.0 C B:ASP610 4.5 92.1 1.0 CA B:LEU612 4.7 95.8 1.0 CG B:PRO611 4.7 92.2 1.0

Chlorine binding site 7 out of 7 in the Nadh 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 Nadh 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:Cl810 b:68.5 occ:1.00 N B:GLU548 3.4 90.2 1.0 CG1 B:VAL552 3.6 85.2 1.0 N B:SER549 3.8 88.6 1.0 CB B:VAL552 3.8 83.9 1.0 CD1 B:TYR547 3.8 89.2 1.0 CA B:TYR547 3.9 90.3 1.0 CB B:SER549 4.0 87.1 1.0 C B:TYR547 4.2 90.0 1.0 CG2 B:VAL552 4.2 83.5 1.0 CB B:TYR547 4.2 89.1 1.0 CA B:GLU548 4.3 90.5 1.0 C B:GLU548 4.4 89.3 1.0 CA B:SER549 4.5 87.1 1.0 CG B:TYR547 4.5 89.3 1.0 CB B:GLU548 4.6 91.8 1.0 NE2 A:GLN163 4.6 74.4 1.0 O B:SER549 4.7 86.1 1.0 CE1 B:TYR547 4.8 89.5 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