Chlorine in PDB 4mvj: 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.

All present enzymatic activity of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.:
1.2.1.12;

The structure of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate., PDB code: 4mvj was solved by G.Minasov, M.Kuhn, I.Dubrovska, J.Winsor, L.Shuvalova, S.Grimshaw, K.Kwon, W.F.Anderson, Center For Structural Genomics Of Infectious Diseases(Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.91 / 2.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	145.879, 69.688, 271.923, 90.00, 98.80, 90.00
R / Rfree (%)	18.6 / 22.4

The structure of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. also contains other interesting chemical elements:

Sodium

(Na)

12 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 - 49;

Binding sites:

The binding sites of Chlorine atom in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. (pdb code 4mvj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 49 binding sites of Chlorine where determined in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate., PDB code: 4mvj:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:66.5 occ:1.00 N A:MET129 3.3 57.9 1.0 CB A:LYS217 3.7 70.0 1.0 CA A:PRO128 3.7 57.6 1.0 C A:PRO128 4.0 55.8 1.0 CB A:MET129 4.1 55.7 1.0 CD A:LYS217 4.2 0.2 1.0 CA A:MET129 4.2 56.5 1.0 O A:THR127 4.3 58.2 1.0 CE A:MET129 4.3 63.6 1.0 CG A:MET129 4.3 59.7 1.0 CG A:LYS217 4.4 77.2 1.0 O A:MET129 4.5 55.8 1.0 O A:LYS217 4.6 77.7 1.0 CB A:PRO128 4.6 57.6 1.0 N A:PRO128 4.7 60.1 1.0 CA A:LYS217 4.8 62.9 1.0 C A:LYS217 4.8 62.1 1.0 C A:THR127 4.9 62.4 1.0 C A:MET129 4.9 55.6 1.0

Chlorine binding site 2 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:71.1 occ:1.00 N A:GLY133 2.8 61.0 1.0 CA A:GLY133 3.3 64.8 1.0 C A:GLY133 3.6 65.7 1.0 N A:ALA134 3.7 64.7 1.0 N A:PHE136 3.8 62.6 1.0 CB A:PHE136 3.8 66.5 1.0 C A:LYS132 3.9 58.1 1.0 O A:HOH538 4.1 62.1 1.0 CA A:LYS132 4.2 55.9 1.0 O A:GLY133 4.3 75.0 1.0 N A:ASN135 4.3 57.5 1.0 CA A:PHE136 4.4 64.7 1.0 C A:ALA134 4.4 57.3 1.0 CG A:PHE136 4.5 60.3 1.0 O A:VAL131 4.5 55.5 1.0 CG A:LYS132 4.6 66.5 1.0 CA A:ALA134 4.6 59.7 1.0 C A:ASN135 4.8 62.4 1.0 CA A:ASN135 4.9 60.7 1.0 N A:ASP137 4.9 65.6 1.0 CD1 A:PHE136 4.9 60.5 1.0 O A:ALA134 5.0 57.2 1.0 CB A:LYS132 5.0 57.2 1.0

Chlorine binding site 3 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:91.8 occ:1.00 CB A:ASP137 3.4 73.8 1.0 CA A:ASP137 3.5 69.1 1.0 N A:ASP137 3.7 65.6 1.0 CE1 A:HIS328 4.2 69.4 1.0 C A:PHE136 4.4 62.2 1.0 CG A:ASP137 4.6 79.5 1.0 CB A:PHE136 4.8 66.5 1.0 O A:PHE136 4.9 59.7 1.0 C A:ASP137 5.0 67.5 1.0

Chlorine binding site 4 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:70.1 occ:1.00 N A:ASP55 3.4 67.2 1.0 CD A:ARG19 3.4 63.0 1.0 CD1 A:PHE54 3.7 64.9 1.0 NE A:ARG19 3.9 67.0 1.0 CB A:ASP55 3.9 75.5 1.0 NZ A:LYS23 4.0 0.5 1.0 CB A:ARG19 4.0 62.4 1.0 CG A:ARG19 4.0 63.9 1.0 CA A:PHE54 4.1 61.3 1.0 NH1 A:ARG19 4.2 64.3 1.0 CE1 A:PHE54 4.2 64.5 1.0 CA A:ASP55 4.2 70.0 1.0 C A:PHE54 4.2 64.3 1.0 CZ A:ARG19 4.4 62.8 1.0 CE A:LYS23 4.4 0.8 1.0 CG A:PHE54 4.6 66.3 1.0 O A:ARG53 4.7 69.1 1.0 CB A:PHE54 4.8 62.2 1.0 O A:ASP55 4.8 69.5 1.0 C A:ASP55 4.9 71.5 1.0 CA A:ARG19 4.9 55.9 1.0 O A:ARG19 5.0 59.2 1.0

Chlorine binding site 5 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl403 b:51.3 occ:1.00 N B:ASP55 3.2 53.7 1.0 CB B:ASP55 3.6 58.3 1.0 CD B:ARG19 3.8 44.4 1.0 NZ B:LYS23 3.9 0.9 1.0 CD1 B:PHE54 3.9 46.2 1.0 CA B:ASP55 3.9 58.9 1.0 CA B:PHE54 4.1 42.9 1.0 C B:PHE54 4.1 43.4 1.0 CE B:LYS23 4.3 0.8 1.0 NH1 B:ARG19 4.3 43.9 1.0 NE B:ARG19 4.4 44.3 1.0 CG B:ARG19 4.4 48.2 1.0 CE1 B:PHE54 4.4 45.8 1.0 CB B:ARG19 4.4 48.3 1.0 O B:ARG53 4.6 45.6 1.0 CZ B:ARG19 4.6 41.2 1.0 O B:ASP55 4.6 71.3 1.0 C B:ASP55 4.6 62.0 1.0 CG B:PHE54 4.6 44.8 1.0 CB B:PHE54 4.9 41.5 1.0 CG B:ASP55 5.0 69.6 1.0

Chlorine binding site 6 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl404 b:71.9 occ:1.00 NH1 B:ARG53 3.3 45.1 1.0 NH2 B:ARG53 3.5 44.1 1.0 CZ B:ARG53 3.9 43.4 1.0 CE1 C:PHE284 4.1 36.3 1.0 CG1 C:VAL292 4.3 35.0 1.0 CB C:THR275 4.4 42.0 1.0 OG1 C:THR275 4.6 41.5 1.0 O C:HOH503 4.8 40.2 1.0 OE1 C:GLU287 4.8 68.6 1.0 O C:TYR274 4.9 38.2 1.0 CZ C:PHE284 4.9 37.5 1.0 CD1 C:PHE284 4.9 36.4 1.0

Chlorine binding site 7 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl405 b:82.0 occ:1.00 N B:VAL58 3.4 65.3 1.0 CG1 B:VAL58 3.5 58.5 1.0 O B:VAL58 3.5 67.9 1.0 CD B:ALY46 4.0 56.0 1.0 CA B:THR57 4.0 63.5 1.0 O B:GLY56 4.1 62.0 1.0 C B:THR57 4.2 62.6 1.0 CA B:VAL58 4.2 59.6 1.0 C B:VAL58 4.3 59.9 1.0 CG B:ALY46 4.3 48.3 1.0 CB B:VAL58 4.5 57.1 1.0 CB B:THR57 4.8 68.6 1.0 CE B:ALY46 4.9 60.4 1.0 C B:GLY56 5.0 57.1 1.0

Chlorine binding site 8 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl406 b:80.2 occ:1.00 N B:GLY133 3.4 59.8 1.0 N B:PHE136 3.5 69.0 1.0 CB B:PHE136 3.6 67.0 1.0 CA B:GLY133 3.8 62.1 1.0 N B:ALA134 3.9 66.0 1.0 C B:GLY133 3.9 68.5 1.0 CA B:PHE136 4.1 69.8 1.0 N B:ASN135 4.2 62.6 1.0 N B:ASP137 4.4 76.8 1.0 C B:LYS132 4.4 56.8 1.0 C B:ALA134 4.5 64.4 1.0 C B:ASN135 4.5 68.4 1.0 CG B:PHE136 4.5 62.0 1.0 CA B:LYS132 4.6 54.9 1.0 O B:GLY133 4.6 69.5 1.0 OD1 B:ASP137 4.6 0.6 1.0 CA B:ASN135 4.7 64.6 1.0 O B:VAL131 4.8 53.2 1.0 CA B:ALA134 4.8 64.5 1.0 C B:PHE136 4.8 73.5 1.0 O B:ALA134 4.9 66.2 1.0 CD1 B:PHE136 5.0 60.0 1.0 CG B:LYS132 5.0 57.3 1.0

Chlorine binding site 9 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl407 b:81.7 occ:1.00 N B:ASP37 3.3 63.2 1.0 OD2 B:ASP37 3.5 81.3 1.0 CG B:ASP37 3.6 78.8 1.0 CD2 B:TYR40 3.8 45.4 1.0 CB B:ASP37 3.8 69.0 1.0 CB B:TYR40 4.0 47.0 1.0 CD2 A:HIS191 4.0 47.3 0.3 CA B:LEU36 4.0 59.8 1.0 CA B:ASP37 4.1 63.7 1.0 CB A:HIS191 4.2 72.5 0.7 C B:LEU36 4.2 60.5 1.0 OD1 B:ASP37 4.2 90.3 1.0 CB A:HIS191 4.3 50.1 0.3 CG B:TYR40 4.3 44.0 1.0 CG A:HIS191 4.5 48.9 0.3 CB B:LEU36 4.6 61.8 1.0 CE2 B:TYR40 4.7 45.8 1.0 CD2 B:LEU36 4.7 69.1 1.0 CA A:HIS191 4.9 69.4 0.7 CA A:HIS191 4.9 53.6 0.3 O B:LEU35 4.9 74.1 1.0 O B:ASP37 5.0 58.1 1.0

Chlorine binding site 10 out of 49 in the 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of 2.85 Angstrom Resolution Crystal Structure of Glyceraldehyde 3- Phosphate Dehydrogenase A (Gapa) From Escherichia Coli Modified By Acetyl Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl408 b:67.8 occ:1.00 N B:MET129 3.1 57.2 1.0 CA B:PRO128 3.7 59.8 1.0 CB B:LYS217 3.8 91.5 1.0 C B:PRO128 3.9 56.1 1.0 CB B:MET129 4.0 54.8 1.0 CA B:MET129 4.1 53.9 1.0 O B:MET129 4.2 51.7 1.0 O B:LYS217 4.3 73.6 1.0 O B:THR127 4.4 59.1 1.0 CG B:MET129 4.4 57.2 1.0 CB B:PRO128 4.5 61.1 1.0 CD B:LYS217 4.5 0.8 1.0 C B:LYS217 4.6 73.7 1.0 CE B:MET129 4.6 63.8 1.0 CG B:LYS217 4.6 0.9 1.0 C B:MET129 4.6 52.8 1.0 CA B:LYS217 4.7 77.8 1.0 N B:PRO128 4.7 61.6 1.0 C B:THR127 5.0 62.2 1.0

M.L.Kuhn, B.Zemaitaitis, L.I.Hu, A.Sahu, D.Sorensen, G.Minasov, B.P.Lima, M.Scholle, M.Mrksich, W.F.Anderson, B.W.Gibson, B.Schilling, A.J.Wolfe. Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation. Plos One V. 9 94816 2014.
ISSN: ESSN 1932-6203
PubMed: 24756028
DOI: 10.1371/JOURNAL.PONE.0094816