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Chlorine in PDB 4eih: Crystal Structure of Arg SH2 Domain

Enzymatic activity of Crystal Structure of Arg SH2 Domain

All present enzymatic activity of Crystal Structure of Arg SH2 Domain:
2.7.10.2;

Protein crystallography data

The structure of Crystal Structure of Arg SH2 Domain, PDB code: 4eih was solved by W.Liu, S.M.Macgrath, A.J.Koleske, T.J.Boggon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.75 / 1.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 56.294, 81.845, 37.686, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 18.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Arg SH2 Domain (pdb code 4eih). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Arg SH2 Domain, PDB code: 4eih:

Chlorine binding site 1 out of 1 in 4eih

Go back to Chlorine Binding Sites List in 4eih
Chlorine binding site 1 out of 1 in the Crystal Structure of Arg SH2 Domain


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 Arg SH2 Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:22.7
occ:0.75
O A:HOH430 2.9 41.6 1.0
O A:HOH421 3.1 31.0 1.0
N A:HIS219 3.3 18.0 1.0
CA A:TYR218 3.9 19.3 1.0
O A:HIS219 4.0 19.9 1.0
NH2 A:ARG180 4.1 39.5 1.0
C A:TYR218 4.1 19.2 1.0
CD2 A:HIS219 4.1 20.3 1.0
CB A:HIS219 4.2 18.8 1.0
CA A:HIS219 4.2 18.4 1.0
O A:VAL217 4.3 21.9 1.0
C A:HIS219 4.5 18.0 1.0
CG A:HIS219 4.5 18.6 1.0
O A:HOH424 4.6 36.6 1.0
CB A:TYR218 4.6 19.4 1.0
CD2 A:TYR218 4.8 19.4 1.0
N A:TYR218 4.9 19.2 1.0

Reference:

S.M.Gifford, W.Liu, C.C.Mader, T.L.Halo, K.Machida, T.J.Boggon, A.J.Koleske. Two Amino Acid Residues Confer Different Binding Affinities of Abelson Family Kinase Src Homology 2 Domains For Phosphorylated Cortactin. J.Biol.Chem. V. 289 19704 2014.
ISSN: ISSN 0021-9258
PubMed: 24891505
DOI: 10.1074/JBC.M114.556480
Page generated: Fri Jul 11 14:51:11 2025

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