Chlorine in PDB 7t1k: Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide

All present enzymatic activity of Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide:
2.7.10.2;

The structure of Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide, PDB code: 7t1k was solved by G.D.Martyn, A.U.Singer, G.Veggiani, I.Kurinov, F.Sicheri, S.S.Sidhu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.23 / 1.25
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	66.08, 66.08, 58.89, 90, 90, 120
R / Rfree (%)	15.2 / 17.8

The structure of Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide (pdb code 7t1k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide, PDB code: 7t1k:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:32.2 occ:1.00 H A:ALA17 2.4 23.6 1.0 HE22 A:GLN35 2.5 29.6 1.0 HB2 A:PRO15 2.8 18.8 1.0 HB2 A:ARG16 3.0 20.5 1.0 H A:ARG16 3.1 19.7 1.0 N A:ALA17 3.2 19.6 1.0 HB2 A:ALA17 3.3 26.0 1.0 NE2 A:GLN35 3.3 24.6 1.0 N A:ARG16 3.5 16.4 1.0 CB A:PRO15 3.7 15.7 1.0 OE1 A:GLN35 3.8 21.1 1.0 HB3 A:ALA17 3.8 26.0 1.0 CB A:ARG16 3.8 17.1 1.0 CB A:ALA17 3.9 21.7 1.0 CA A:ARG16 4.0 16.6 1.0 HE21 A:GLN35 4.0 29.6 1.0 CD A:GLN35 4.0 20.7 1.0 HB3 A:PRO15 4.0 18.8 1.0 C A:ARG16 4.0 18.3 1.0 CA A:ALA17 4.1 21.4 1.0 C A:PRO15 4.2 14.6 1.0 HB3 A:ARG16 4.3 20.5 1.0 O A:HOH398 4.4 44.2 1.0 O A:HOH399 4.4 57.1 1.0 CA A:PRO15 4.4 14.6 1.0 HG2 A:PRO15 4.5 19.7 1.0 HA A:ALA17 4.6 25.7 1.0 HA A:PRO15 4.6 17.5 1.0 CG A:PRO15 4.7 16.4 1.0 HG3 A:ARG16 4.7 20.1 1.0 HB1 A:ALA17 4.8 26.0 1.0 CG A:ARG16 4.8 16.7 1.0 HA A:ARG16 4.9 19.9 1.0 HD2 A:ARG16 4.9 21.2 1.0 HG3 A:PRO15 4.9 19.7 1.0 H A:GLU18 5.0 25.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of A Superbinder Fes SH2 Domain (SFES1) in Complex with A High Affinity Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:47.2 occ:1.00 HD1 A:HIS5 2.2 24.8 1.0 H A:HIS5 2.4 16.7 1.0 O A:HOH381 2.7 39.8 1.0 HB3 A:LEU4 2.8 16.1 1.0 HB3 A:HIS5 3.0 20.3 1.0 ND1 A:HIS5 3.0 20.6 1.0 N A:HIS5 3.2 13.9 1.0 H A:LEU4 3.4 17.4 1.0 HB3 A:PRO3 3.5 23.2 1.0 HB2 A:PRO3 3.6 23.2 1.0 N A:LEU4 3.6 14.5 1.0 CB A:HIS5 3.7 16.9 1.0 CB A:LEU4 3.7 13.4 1.0 CG A:HIS5 3.8 19.4 1.0 CB A:PRO3 4.0 19.3 1.0 CA A:LEU4 4.0 13.2 1.0 CA A:HIS5 4.0 14.6 1.0 C A:LEU4 4.0 12.3 1.0 CE1 A:HIS5 4.1 20.8 1.0 HD23 A:LEU4 4.2 15.8 1.0 C A:PRO3 4.3 15.3 1.0 HB2 A:LEU4 4.3 16.1 1.0 HE1 A:HIS5 4.3 24.9 1.0 HG A:LEU4 4.4 15.6 1.0 HA A:HIS5 4.5 17.5 1.0 CA A:PRO3 4.5 18.0 1.0 HA A:PRO3 4.6 21.6 1.0 HB2 A:HIS5 4.6 20.3 1.0 CG A:LEU4 4.6 13.0 1.0 CD2 A:LEU4 4.9 13.2 1.0 OH A:TYR40 4.9 16.3 1.0 H A:GLU6 4.9 16.9 1.0 HA A:LEU4 5.0 15.8 1.0 HH A:TYR40 5.0 19.6 1.0 O A:HOH376 5.0 43.6 1.0

G.D.Martyn, G.Veggiani, U.Kusebauch, S.R.Morrone, B.P.Yates, A.U.Singer, J.Tong, N.Manczyk, G.Gish, Z.Sun, I.Kurinov, F.Sicheri, M.F.Moran, R.L.Moritz, S.S.Sidhu. Engineered SH2 Domains For Targeted Phosphoproteomics. Acs Chem.Biol. V. 17 1472 2022.
ISSN: ESSN 1554-8937
PubMed: 35613471
DOI: 10.1021/ACSCHEMBIO.2C00051