Manganese in PDB 2qc8: Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate

All present enzymatic activity of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate:
6.3.1.2;

The structure of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate, PDB code: 2qc8 was solved by T.Karlberg, L.Lehtio, C.H.Arrowsmith, H.Berglund, R.D.Busam, R.Collins, L.G.Dahlgren, A.Edwards, S.Flodin, A.Flores, S.Graslund, M.Hammarstrom, M.Hogbom, I.Johansson, A.Kallas, T.Kotenyova, M.Moche, P.Nordlund, T.Nyman, C.Persson, J.Sagemark, M.Sundstrom, A.G.Thorsell, S.Van Denberg, J.Weigelt, L.Holmberg-Schiavone, Structural Genomics Consortium(Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.94 / 2.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	181.210, 126.080, 188.170, 90.00, 92.14, 90.00
R / Rfree (%)	16.6 / 21.7

The structure of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate also contains other interesting chemical elements:

Chlorine

(Cl)

10 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30;

Binding sites:

The binding sites of Manganese atom in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate (pdb code 2qc8). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 30 binding sites of Manganese where determined in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate, PDB code: 2qc8:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Manganese binding site 1 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:37.8 occ:1.00 OE1 A:GLU203 2.0 39.7 1.0 O A:HOH704 2.0 35.8 1.0 OE2 A:GLU136 2.1 42.7 1.0 OE1 A:GLU196 2.2 36.9 1.0 NE A:P3S601 2.2 35.5 1.0 O3A A:P3S601 2.4 31.5 1.0 PA A:P3S601 2.9 33.8 1.0 CD A:GLU203 3.0 38.6 1.0 CD A:GLU136 3.1 39.6 1.0 CD A:GLU196 3.1 39.0 1.0 OE2 A:GLU203 3.6 39.9 1.0 CG A:GLU136 3.6 38.5 1.0 SD A:P3S601 3.6 33.5 1.0 MN A:MN403 3.7 40.7 1.0 CG A:GLU196 3.8 37.8 1.0 O2A A:P3S601 3.9 36.6 1.0 OE2 A:GLU196 4.0 39.6 1.0 CG A:P3S601 4.0 34.7 1.0 O1A A:P3S601 4.1 33.5 1.0 OE1 A:GLU136 4.1 38.8 1.0 OE1 A:GLU134 4.1 41.5 1.0 CB A:P3S601 4.2 33.6 1.0 CG A:GLU203 4.2 39.0 1.0 CE1 A:HIS253 4.3 38.1 1.0 CE A:P3S601 4.3 34.8 1.0 O A:HOH729 4.4 40.0 1.0 ND2 A:ASN194 4.5 34.1 1.0 CB A:GLU203 4.6 39.2 1.0 ND1 A:HIS253 4.7 38.7 1.0 OE A:P3S601 4.7 35.0 1.0 MN A:MN402 4.8 37.8 1.0 O1B A:ADP501 5.0 31.5 1.0

Manganese binding site 2 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:37.8 occ:1.00 OE2 A:GLU338 2.0 43.2 1.0 O2A A:P3S601 2.0 36.6 1.0 O3B A:ADP501 2.1 35.9 1.0 OE1 A:GLU134 2.3 41.5 1.0 ND1 A:HIS253 2.4 38.7 1.0 OE2 A:GLU134 2.5 40.3 1.0 CD A:GLU134 2.7 40.8 1.0 PA A:P3S601 3.2 33.8 1.0 CD A:GLU338 3.2 42.6 1.0 CE1 A:HIS253 3.2 38.1 1.0 PB A:ADP501 3.3 35.0 1.0 O3A A:P3S601 3.3 31.5 1.0 O1B A:ADP501 3.4 31.5 1.0 CG A:HIS253 3.5 38.3 1.0 NH1 A:ARG340 3.5 41.9 1.0 MN A:MN403 3.7 40.7 1.0 O A:HOH704 3.9 35.8 1.0 NH1 A:ARG324 3.9 48.2 1.0 CB A:HIS253 3.9 39.0 1.0 OE1 A:GLU338 3.9 42.9 1.0 O A:HOH730 4.0 31.4 1.0 CG A:GLU134 4.2 41.5 1.0 O3A A:ADP501 4.3 31.2 1.0 CG A:GLU338 4.3 42.7 1.0 O1A A:P3S601 4.3 33.5 1.0 NE A:P3S601 4.3 35.5 1.0 NE2 A:HIS253 4.4 37.2 1.0 O2B A:ADP501 4.4 34.8 1.0 CD2 A:HIS253 4.5 37.5 1.0 O2A A:ADP501 4.6 35.2 1.0 CZ A:ARG340 4.7 40.8 1.0 CB A:GLU134 4.8 39.9 1.0 MN A:MN401 4.8 37.8 1.0

Manganese binding site 3 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn403 b:40.7 occ:1.00 O3A A:P3S601 2.0 31.5 1.0 O2A A:ADP501 2.0 35.2 1.0 O A:HOH729 2.1 40.0 1.0 O1B A:ADP501 2.1 31.5 1.0 OE1 A:GLU134 2.1 41.5 1.0 OE2 A:GLU203 2.2 39.9 1.0 CD A:GLU203 3.1 38.6 1.0 CD A:GLU134 3.2 40.8 1.0 PB A:ADP501 3.2 35.0 1.0 OE1 A:GLU203 3.3 39.7 1.0 PA A:ADP501 3.3 37.3 1.0 PA A:P3S601 3.4 33.8 1.0 O A:HOH704 3.6 35.8 1.0 O3A A:ADP501 3.6 31.2 1.0 MN A:MN401 3.7 37.8 1.0 O3B A:ADP501 3.7 35.9 1.0 MN A:MN402 3.7 37.8 1.0 O2A A:P3S601 3.9 36.6 1.0 O A:HOH731 3.9 26.9 1.0 CG A:GLU134 3.9 41.5 1.0 OE2 A:GLU134 4.1 40.3 1.0 NE2 A:GLN205 4.1 36.7 1.0 O1A A:P3S601 4.2 33.5 1.0 O1A A:ADP501 4.3 40.1 1.0 OD1 A:ASN194 4.3 34.9 1.0 CB A:GLU134 4.4 39.9 1.0 NE A:P3S601 4.4 35.5 1.0 O5' A:ADP501 4.4 37.0 1.0 CG A:GLU203 4.5 39.0 1.0 O2B A:ADP501 4.5 34.8 1.0 CD A:GLN205 4.7 38.0 1.0 CG A:GLN205 4.8 37.6 1.0 OE1 A:GLU196 5.0 36.9 1.0

Manganese binding site 4 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:32.0 occ:1.00 OE1 B:GLU203 2.0 39.8 1.0 OE2 B:GLU136 2.1 37.8 1.0 O B:HOH744 2.1 29.6 1.0 OE1 B:GLU196 2.2 40.0 1.0 O3A B:P3S601 2.3 29.3 1.0 NE B:P3S601 2.4 27.5 1.0 PA B:P3S601 2.9 28.6 1.0 CD B:GLU203 3.0 39.0 1.0 CD B:GLU136 3.1 39.3 1.0 CD B:GLU196 3.2 41.4 1.0 OE2 B:GLU203 3.5 39.4 1.0 SD B:P3S601 3.5 27.3 1.0 MN B:MN403 3.6 31.6 1.0 CG B:GLU136 3.7 38.3 1.0 CG B:GLU196 3.8 39.1 1.0 O2A B:P3S601 3.9 32.7 1.0 O1A B:P3S601 4.0 30.4 1.0 CE B:P3S601 4.0 27.8 1.0 OE1 B:GLU134 4.1 41.2 1.0 CG B:P3S601 4.1 27.7 1.0 OE1 B:GLU136 4.1 37.5 1.0 OE2 B:GLU196 4.1 43.2 1.0 CG B:GLU203 4.2 38.6 1.0 CB B:P3S601 4.2 27.3 1.0 CE1 B:HIS253 4.4 37.0 1.0 ND2 B:ASN194 4.6 38.2 1.0 O B:HOH741 4.6 22.3 1.0 CB B:GLU203 4.7 38.9 1.0 ND1 B:HIS253 4.7 38.3 1.0 OE B:P3S601 4.8 30.4 1.0 MN B:MN402 4.9 34.4 1.0 O3B B:ADP501 5.0 31.4 1.0

Manganese binding site 5 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn402 b:34.4 occ:1.00 OE2 B:GLU338 2.0 47.8 1.0 O2B B:ADP501 2.1 35.9 1.0 O2A B:P3S601 2.1 32.7 1.0 OE1 B:GLU134 2.2 41.2 1.0 OE2 B:GLU134 2.3 39.5 1.0 ND1 B:HIS253 2.3 38.3 1.0 CD B:GLU134 2.6 40.5 1.0 CD B:GLU338 3.2 43.7 1.0 CE1 B:HIS253 3.2 37.0 1.0 PB B:ADP501 3.3 35.1 1.0 CG B:HIS253 3.4 37.6 1.0 PA B:P3S601 3.4 28.6 1.0 O3B B:ADP501 3.5 31.4 1.0 O3A B:P3S601 3.6 29.3 1.0 CB B:HIS253 3.7 38.9 1.0 MN B:MN403 3.7 31.6 1.0 NH1 B:ARG340 3.7 41.8 1.0 O B:HOH744 3.8 29.6 1.0 NH1 B:ARG324 4.0 46.2 1.0 OE1 B:GLU338 4.0 43.0 1.0 O B:HOH742 4.0 27.9 1.0 CG B:GLU134 4.1 40.0 1.0 CG B:GLU338 4.1 43.2 1.0 O3A B:ADP501 4.1 29.3 1.0 NE B:P3S601 4.3 27.5 1.0 NE2 B:HIS253 4.4 34.8 1.0 O2A B:ADP501 4.5 31.4 1.0 CD2 B:HIS253 4.5 36.1 1.0 O1A B:P3S601 4.5 30.4 1.0 O1B B:ADP501 4.5 29.2 1.0 CB B:GLU134 4.7 39.1 1.0 CZ B:ARG340 4.8 40.4 1.0 PA B:ADP501 4.9 32.6 1.0 MN B:MN401 4.9 32.0 1.0

Manganese binding site 6 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn403 b:31.6 occ:1.00 O3A B:P3S601 1.9 29.3 1.0 O3B B:ADP501 2.0 31.4 1.0 O2A B:ADP501 2.1 31.4 1.0 OE2 B:GLU203 2.1 39.4 1.0 OE1 B:GLU134 2.3 41.2 1.0 O B:HOH741 2.4 22.3 1.0 CD B:GLU203 3.1 39.0 1.0 PB B:ADP501 3.2 35.1 1.0 CD B:GLU134 3.2 40.5 1.0 PA B:P3S601 3.3 28.6 1.0 PA B:ADP501 3.4 32.6 1.0 OE1 B:GLU203 3.4 39.8 1.0 O B:HOH744 3.5 29.6 1.0 MN B:MN401 3.6 32.0 1.0 O2A B:P3S601 3.6 32.7 1.0 O3A B:ADP501 3.7 29.3 1.0 MN B:MN402 3.7 34.4 1.0 O2B B:ADP501 3.7 35.9 1.0 CG B:GLU134 4.0 40.0 1.0 OE2 B:GLU134 4.1 39.5 1.0 O1A B:P3S601 4.1 30.4 1.0 O A:HOH732 4.2 26.3 1.0 NE2 B:GLN205 4.2 36.2 1.0 OD1 B:ASN194 4.3 34.4 1.0 CB B:GLU134 4.4 39.1 1.0 O1A B:ADP501 4.4 31.9 1.0 NE B:P3S601 4.4 27.5 1.0 O5' B:ADP501 4.5 31.9 1.0 CG B:GLU203 4.5 38.6 1.0 O1B B:ADP501 4.6 29.2 1.0 CD B:GLN205 4.8 37.8 1.0 CG B:GLN205 4.9 37.1 1.0

Manganese binding site 7 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn401 b:31.9 occ:1.00 OE1 C:GLU203 2.0 41.3 1.0 O3A C:P3S601 2.1 30.4 1.0 OE2 C:GLU136 2.1 38.1 1.0 OE1 C:GLU196 2.1 36.2 1.0 O C:HOH740 2.2 23.9 1.0 NE C:P3S601 2.7 29.2 1.0 CD C:GLU196 3.0 38.0 1.0 PA C:P3S601 3.1 31.6 1.0 CD C:GLU136 3.1 39.4 1.0 CD C:GLU203 3.1 39.1 1.0 SD C:P3S601 3.5 27.7 1.0 CG C:GLU136 3.6 38.4 1.0 MN C:MN403 3.7 31.8 1.0 OE2 C:GLU203 3.7 40.0 1.0 CG C:GLU196 3.7 35.6 1.0 OE2 C:GLU196 3.8 40.3 1.0 CG C:P3S601 3.9 26.9 1.0 CE C:P3S601 3.9 24.4 1.0 O1A C:P3S601 3.9 31.4 1.0 O2A C:P3S601 4.1 28.7 1.0 OE1 C:GLU136 4.1 40.8 1.0 CG C:GLU203 4.2 38.2 1.0 OE1 C:GLU134 4.2 42.8 1.0 CB C:P3S601 4.2 24.5 1.0 CE1 C:HIS253 4.3 38.0 1.0 O C:HOH741 4.5 27.1 1.0 ND2 C:ASN194 4.6 36.1 1.0 CB C:GLU203 4.6 38.5 1.0 ND1 C:HIS253 4.6 39.3 1.0 O C:HOH738 4.7 20.6 1.0 OE C:P3S601 4.9 34.4 1.0 N C:P3S601 5.0 24.9 1.0 OD1 C:ASN194 5.0 36.0 1.0 O C:HOH730 5.0 31.0 1.0 MN C:MN402 5.0 33.2 1.0

Manganese binding site 8 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn402 b:33.2 occ:1.00 OE2 C:GLU338 1.9 44.4 1.0 O2A C:P3S601 2.0 28.7 1.0 O2B C:ADP501 2.1 24.3 1.0 OE2 C:GLU134 2.3 43.2 1.0 ND1 C:HIS253 2.3 39.3 1.0 OE1 C:GLU134 2.4 42.8 1.0 CD C:GLU134 2.7 41.6 1.0 CD C:GLU338 3.2 43.7 1.0 CE1 C:HIS253 3.2 38.0 1.0 CG C:HIS253 3.3 37.9 1.0 PB C:ADP501 3.3 28.0 1.0 PA C:P3S601 3.3 31.6 1.0 O3B C:ADP501 3.4 28.1 1.0 O3A C:P3S601 3.6 30.4 1.0 NH1 C:ARG340 3.6 43.7 1.0 CB C:HIS253 3.6 39.7 1.0 MN C:MN403 3.7 31.8 1.0 OE1 C:GLU338 3.9 42.6 1.0 O C:HOH740 3.9 23.9 1.0 O C:HOH736 4.0 32.0 1.0 NH1 C:ARG324 4.0 47.0 1.0 NE C:P3S601 4.0 29.2 1.0 O3A C:ADP501 4.1 28.5 1.0 CG C:GLU134 4.1 41.3 1.0 CG C:GLU338 4.3 43.1 1.0 NE2 C:HIS253 4.3 36.1 1.0 CD2 C:HIS253 4.4 38.1 1.0 O1A C:P3S601 4.5 31.4 1.0 O1B C:ADP501 4.6 25.2 1.0 O2A C:ADP501 4.6 23.6 1.0 CZ C:ARG340 4.6 40.9 1.0 CB C:GLU134 4.7 40.3 1.0 MN C:MN401 5.0 31.9 1.0

Manganese binding site 9 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 9 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn403 b:31.8 occ:1.00 OE1 C:GLU134 2.0 42.8 1.0 O3A C:P3S601 2.2 30.4 1.0 O2A C:ADP501 2.2 23.6 1.0 O3B C:ADP501 2.3 28.1 1.0 OE2 C:GLU203 2.3 40.0 1.0 O C:HOH738 2.3 20.6 1.0 CD C:GLU203 3.0 39.1 1.0 CD C:GLU134 3.1 41.6 1.0 OE1 C:GLU203 3.1 41.3 1.0 PA C:P3S601 3.3 31.6 1.0 PB C:ADP501 3.4 28.0 1.0 O2A C:P3S601 3.5 28.7 1.0 PA C:ADP501 3.5 30.1 1.0 O C:HOH740 3.5 23.9 1.0 O3A C:ADP501 3.6 28.5 1.0 MN C:MN401 3.7 31.9 1.0 MN C:MN402 3.7 33.2 1.0 O2B C:ADP501 3.8 24.3 1.0 CG C:GLU134 3.9 41.3 1.0 O1A C:P3S601 3.9 31.4 1.0 OE2 C:GLU134 4.1 43.2 1.0 O C:HOH709 4.1 23.0 1.0 OD1 C:ASN194 4.2 36.0 1.0 NE2 C:GLN205 4.3 37.1 1.0 CB C:GLU134 4.3 40.3 1.0 O5' C:ADP501 4.4 29.8 1.0 CG C:GLU203 4.5 38.2 1.0 NE C:P3S601 4.5 29.2 1.0 O1A C:ADP501 4.5 25.2 1.0 O1B C:ADP501 4.6 25.2 1.0 CD C:GLN205 4.7 37.7 1.0 CG C:GLN205 4.8 38.3 1.0 OE1 C:GLU196 4.9 36.2 1.0 ND1 C:HIS253 5.0 39.3 1.0

Manganese binding site 10 out of 30 in the Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 10 of Crystal Structure of Human Glutamine Synthetase in Complex with Adp and Methionine Sulfoximine Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn401 b:31.7 occ:1.00 OE2 D:GLU136 2.2 39.8 1.0 OE1 D:GLU203 2.2 39.8 1.0 O3A D:P3S601 2.2 27.6 1.0 OE1 D:GLU196 2.3 39.8 1.0 NE D:P3S601 2.3 29.5 1.0 PA D:P3S601 2.8 28.1 1.0 CD D:GLU196 3.2 40.2 1.0 CD D:GLU136 3.2 38.7 1.0 CD D:GLU203 3.2 38.0 1.0 SD D:P3S601 3.5 29.8 1.0 MN D:MN403 3.7 30.9 1.0 OE2 D:GLU203 3.7 37.1 1.0 CG D:GLU136 3.7 38.7 1.0 CE D:P3S601 3.9 30.9 1.0 O1A D:P3S601 3.9 30.3 1.0 CG D:GLU196 3.9 38.4 1.0 O2A D:P3S601 3.9 33.7 1.0 CG D:P3S601 3.9 30.4 1.0 OE2 D:GLU196 4.0 40.0 1.0 OE1 D:GLU134 4.1 44.5 1.0 OE1 D:GLU136 4.2 38.1 1.0 CE1 D:HIS253 4.3 38.4 1.0 CB D:P3S601 4.3 29.1 1.0 CG D:GLU203 4.4 37.7 1.0 O D:HOH709 4.6 33.1 1.0 ND2 D:ASN194 4.6 33.1 1.0 ND1 D:HIS253 4.7 38.1 1.0 CB D:GLU203 4.8 38.5 1.0 OE D:P3S601 4.8 30.2 1.0 O3B D:ADP501 4.9 30.4 1.0 O D:HOH747 4.9 20.3 1.0 MN D:MN402 4.9 35.4 1.0

W.W.Krajewski, R.Collins, L.Holmberg-Schiavone, T.A.Jones, T.Karlberg, S.L.Mowbray. Crystal Structures of Mammalian Glutamine Synthetases Illustrate Substrate-Induced Conformational Changes and Provide Opportunities For Drug and Herbicide Design. J.Mol.Biol. V. 375 217 2008.
ISSN: ISSN 0022-2836
PubMed: 18005987
DOI: 10.1016/J.JMB.2007.10.029