Chlorine in PDB 6fl5: Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution

All present enzymatic activity of Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution:
2.1.2.1;

The structure of Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution, PDB code: 6fl5 was solved by G.Giardina, F.Cutruzzola, R.Lucchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.01 / 3.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	139.719, 139.719, 267.377, 90.00, 90.00, 90.00
R / Rfree (%)	26.2 / 27.7

The binding sites of Chlorine atom in the Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution (pdb code 6fl5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution, PDB code: 6fl5:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:19.0 occ:1.00 OG A:SER203 3.1 66.2 1.0 OH D:TYR83 3.3 87.1 1.0 CB A:SER53 4.0 70.3 1.0 OG A:SER53 4.0 69.6 1.0 O3 A:PLP501 4.0 60.7 1.0 C4A A:PLP501 4.0 61.1 1.0 CE1 A:HIS231 4.0 52.2 1.0 NH1 A:ARG402 4.0 68.5 1.0 OE2 D:GLU75 4.1 89.7 1.0 NZ A:LYS257 4.2 62.0 1.0 NH2 A:ARG402 4.2 69.0 1.0 CD2 A:HIS148 4.4 61.9 1.0 CE A:LYS257 4.5 63.5 1.0 CB A:SER203 4.5 66.2 1.0 CZ D:TYR83 4.5 87.9 1.0 NE2 A:HIS148 4.6 62.4 1.0 CZ A:ARG402 4.6 68.1 1.0 C3 A:PLP501 4.7 60.3 1.0 C4 A:PLP501 4.8 60.7 1.0 CD D:GLU75 4.8 87.9 1.0 NE2 A:HIS231 4.9 51.9 1.0 CE2 D:TYR83 4.9 87.8 1.0 CE1 D:TYR73 4.9 71.7 1.0 OE1 D:GLU75 4.9 88.3 1.0 CZ D:TYR73 4.9 71.9 1.0 ND1 A:HIS231 4.9 52.1 1.0

Chlorine binding site 2 out of 4 in the Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:32.9 occ:1.00 OH A:TYR83 2.8 78.2 1.0 OG D:SER203 3.3 58.3 1.0 NH2 D:ARG402 3.9 58.8 1.0 NH1 D:ARG402 3.9 58.1 1.0 OG D:SER53 3.9 61.4 1.0 OE2 A:GLU75 4.0 80.9 1.0 CB D:SER53 4.0 61.4 1.0 CZ A:TYR83 4.1 79.2 1.0 C4A D:PLP500 4.2 65.8 1.0 O3 D:PLP500 4.2 65.4 1.0 CE1 D:HIS231 4.2 69.7 1.0 CZ D:ARG402 4.4 57.8 1.0 OE1 A:GLU75 4.5 81.0 1.0 CD A:GLU75 4.6 79.8 1.0 CE2 A:TYR83 4.6 79.5 1.0 NZ D:LYS257 4.6 64.0 1.0 CB D:SER203 4.7 57.3 1.0 CD2 D:HIS148 4.7 56.7 1.0 CE D:LYS257 4.8 63.0 1.0 CE1 A:TYR73 4.9 72.6 1.0 NE2 D:HIS148 5.0 57.5 1.0

Chlorine binding site 3 out of 4 in the Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl502 b:42.6 occ:1.00 OH G:TYR83 3.4 87.7 1.0 OG J:SER53 3.5 88.7 1.0 CB J:SER53 3.6 88.3 1.0 OG J:SER203 3.6 73.4 1.0 NH2 J:ARG402 3.8 90.8 1.0 NH1 J:ARG402 3.9 90.8 1.0 C4A J:PLP501 4.2 72.2 1.0 CE1 J:HIS231 4.2 78.6 1.0 CZ J:ARG402 4.3 90.8 1.0 O3 J:PLP501 4.5 69.9 1.0 NZ J:LYS257 4.6 72.3 1.0 CZ G:TYR83 4.6 88.2 1.0 CE J:LYS257 4.6 71.0 1.0 OE2 G:GLU75 4.7 88.6 1.0 NE2 J:HIS231 4.9 78.5 1.0 CZ G:TYR73 5.0 91.8 1.0

Chlorine binding site 4 out of 4 in the Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of Human SHMT1-H135N-R137A-E168N Mutant at 3.6 Ang. Resolution within 5.0Å range: probe atom residue distance (Å) B Occ J:Cl502 b:20.3 occ:1.00 OH J:TYR83 3.3 88.4 1.0 OG G:SER203 3.5 73.2 1.0 CB G:SER53 3.6 76.8 1.0 OG G:SER53 3.7 76.2 1.0 CE1 G:HIS231 3.9 58.9 1.0 NH2 G:ARG402 4.0 70.9 1.0 NH1 G:ARG402 4.0 69.9 1.0 C4A G:PLP501 4.1 70.0 1.0 NZ G:LYS257 4.2 71.2 1.0 O3 G:PLP501 4.2 68.0 1.0 CE G:LYS257 4.3 71.1 1.0 CZ G:ARG402 4.5 70.7 1.0 CZ J:TYR83 4.5 88.5 1.0 OE2 J:GLU75 4.6 97.0 1.0 NE2 G:HIS231 4.8 59.2 1.0 CZ J:TYR73 4.8 82.4 1.0 CD2 G:HIS148 4.9 82.9 1.0 ND1 G:HIS231 4.9 59.3 1.0 CE1 J:TYR73 4.9 83.1 1.0 CB G:SER203 4.9 72.0 1.0 OH J:TYR73 4.9 81.1 1.0 C4 G:PLP501 5.0 69.4 1.0 CE2 J:TYR83 5.0 87.2 1.0 C3 G:PLP501 5.0 68.4 1.0

G.Giardina, A.Paone, A.Tramonti, R.Lucchi, M.Marani, M.C.Magnifico, A.Bouzidi, V.Pontecorvi, G.Guiducci, C.Zamparelli, S.Rinaldo, A.Paiardini, R.Contestabile, F.Cutruzzola. The Catalytic Activity of Serine Hydroxymethyltransferase Is Essential For De Novo Nuclear Dtmp Synthesis in Lung Cancer Cells. Febs J. V. 285 3238 2018.
ISSN: ISSN 1742-4658
PubMed: 30035852
DOI: 10.1111/FEBS.14610