Zinc in PDB 1btk: pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C

All present enzymatic activity of pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C:
2.7.1.112;

The structure of pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C, PDB code: 1btk was solved by M.Hyvonen, M.Saraste, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.50 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.150, 59.870, 55.940, 90.00, 98.21, 90.00
R / Rfree (%)	23.1 / 28.2

The structure of pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Zinc atom in the pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C (pdb code 1btk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C, PDB code: 1btk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:13.2 occ:1.00 ND1 A:HIS143 2.1 15.1 1.0 SG A:CYS165 2.2 16.4 1.0 SG A:CYS155 2.4 14.0 1.0 SG A:CYS154 2.4 13.7 1.0 CE1 A:HIS143 3.0 16.8 1.0 CG A:HIS143 3.1 15.4 1.0 CB A:CYS155 3.3 18.0 1.0 CB A:CYS165 3.3 19.1 1.0 CB A:HIS143 3.5 11.8 1.0 CB A:CYS154 3.5 16.4 1.0 N A:CYS155 3.6 20.3 1.0 CA A:HIS143 3.8 11.3 1.0 CB A:TYR152 4.0 16.4 1.0 C A:CYS154 4.0 19.2 1.0 N A:CYS165 4.0 18.2 1.0 CA A:CYS155 4.1 19.7 1.0 NE2 A:HIS143 4.2 17.2 1.0 CD2 A:HIS143 4.2 15.8 1.0 CA A:CYS154 4.2 16.9 1.0 CG A:TYR152 4.3 15.8 1.0 CA A:CYS165 4.3 18.3 1.0 CD A:PRO144 4.4 14.6 1.0 N A:CYS154 4.7 16.5 1.0 CD1 A:TYR152 4.7 15.4 1.0 C A:HIS143 4.8 12.9 1.0 O A:CYS154 4.8 20.7 1.0 CD2 A:TYR152 4.8 16.8 1.0 N A:HIS143 4.8 10.4 1.0 NE2 A:GLN157 4.9 21.9 1.0 N A:PRO144 4.9 13.3 1.0 O A:TYR142 5.0 12.6 1.0

Zinc binding site 2 out of 2 in the pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of pH Domain and Btk Motif From Bruton'S Tyrosine Kinase Mutant R28C within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn180 b:19.2 occ:1.00 ND1 B:HIS143 2.0 17.2 1.0 SG B:CYS165 2.2 21.7 1.0 SG B:CYS154 2.3 20.1 1.0 SG B:CYS155 2.4 21.4 1.0 CE1 B:HIS143 3.0 17.8 1.0 CG B:HIS143 3.1 17.5 1.0 CB B:CYS165 3.2 25.2 1.0 CB B:CYS155 3.4 21.6 1.0 CB B:HIS143 3.5 13.1 1.0 CB B:CYS154 3.5 20.5 1.0 N B:CYS155 3.6 21.9 1.0 CA B:HIS143 3.8 14.1 1.0 N B:CYS165 4.0 21.0 1.0 CB B:TYR152 4.0 20.3 1.0 CA B:CYS155 4.1 22.9 1.0 C B:CYS154 4.1 22.2 1.0 NE2 B:HIS143 4.2 17.8 1.0 CD2 B:HIS143 4.2 17.7 1.0 CA B:CYS165 4.2 22.8 1.0 CA B:CYS154 4.3 21.1 1.0 CG B:TYR152 4.3 16.8 1.0 CD B:PRO144 4.5 15.9 1.0 N B:CYS154 4.7 20.7 1.0 CD1 B:TYR152 4.8 15.4 1.0 C B:HIS143 4.8 15.4 1.0 CD2 B:TYR152 4.8 16.2 1.0 N B:HIS143 4.9 13.9 1.0 O B:TYR142 4.9 16.9 1.0 N B:PRO144 5.0 15.5 1.0

M.Hyvonen, M.Saraste. Structure of the pH Domain and Btk Motif From Bruton'S Tyrosine Kinase: Molecular Explanations For X-Linked Agammaglobulinaemia. Embo J. V. 16 3396 1997.
ISSN: ISSN 0261-4189
PubMed: 9218782
DOI: 10.1093/EMBOJ/16.12.3396