Zinc in PDB 1b55: pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate

All present enzymatic activity of pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate:
2.7.1.112;

The structure of pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate, PDB code: 1b55 was solved by K.Djinovic Carugo, E.Baraldi, M.Hyvoenen, P.Lo Surdo, A.M.Riley, B.V.L.Potter, R.O'brien, J.E.Ladbury, M.Saraste, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.40
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	110.205, 110.205, 215.528, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate (pdb code 1b55). 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 From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate, PDB code: 1b55:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:45.4 occ:1.00 ND1 A:HIS143 1.9 52.8 1.0 SG A:CYS165 2.0 45.0 1.0 SG A:CYS155 2.3 53.4 1.0 SG A:CYS154 2.4 44.3 1.0 CE1 A:HIS143 2.8 55.5 1.0 CG A:HIS143 3.0 52.5 1.0 CB A:CYS155 3.2 57.1 1.0 CB A:CYS165 3.3 41.7 1.0 CB A:HIS143 3.4 45.0 1.0 CB A:CYS154 3.5 40.1 1.0 N A:CYS155 3.6 61.5 1.0 N A:CYS165 3.6 42.4 1.0 CA A:HIS143 3.8 46.9 1.0 NE2 A:HIS143 4.0 54.5 1.0 CA A:CYS165 4.1 39.0 1.0 CA A:CYS155 4.1 58.5 1.0 CD2 A:HIS143 4.1 54.3 1.0 C A:CYS154 4.1 58.2 1.0 CA A:CYS154 4.2 47.2 1.0 CB A:TYR152 4.3 44.4 1.0 C A:GLY164 4.5 49.0 1.0 N A:CYS154 4.5 48.4 1.0 CG A:TYR152 4.6 41.0 1.0 O A:TYR142 4.7 47.9 1.0 CA A:GLY164 4.7 51.5 1.0 CD A:PRO144 4.7 37.5 1.0 N A:HIS143 4.7 45.9 1.0 CD1 A:TYR152 4.9 41.1 1.0 C A:HIS143 4.9 49.2 1.0 O A:CYS154 4.9 50.7 1.0 NE2 A:GLN157 4.9 80.6 1.0 O A:MET163 5.0 73.4 1.0 C A:CYS165 5.0 50.5 1.0

Zinc binding site 2 out of 2 in the pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3, 4,5-Tetrakisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn171 b:85.0 occ:1.00 ND1 B:HIS143 2.4 74.2 1.0 CB B:CYS154 2.4 60.0 1.0 SG B:CYS165 2.7 73.1 1.0 CB B:HIS143 2.9 70.1 1.0 CG B:HIS143 3.0 76.6 1.0 CA B:HIS143 3.0 64.2 1.0 O B:CYS165 3.1 67.7 1.0 N B:CYS165 3.1 58.7 1.0 CB B:CYS165 3.1 67.1 1.0 CA B:CYS165 3.2 61.2 1.0 SG B:CYS154 3.2 70.3 1.0 C B:CYS165 3.3 70.8 1.0 O B:TYR142 3.3 67.7 1.0 CA B:CYS154 3.3 62.2 1.0 C B:CYS154 3.4 75.8 1.0 SG B:CYS155 3.4 85.0 1.0 CE1 B:HIS143 3.6 77.6 1.0 N B:CYS155 3.7 72.9 1.0 CD B:PRO144 3.9 60.9 1.0 N B:HIS143 3.9 56.8 1.0 O B:CYS154 4.0 74.3 1.0 C B:TYR142 4.0 66.4 1.0 C B:HIS143 4.1 70.5 1.0 C B:GLY164 4.2 70.6 1.0 CD2 B:HIS143 4.3 81.1 1.0 N B:GLN166 4.3 59.3 1.0 NE2 B:HIS143 4.5 80.3 1.0 SG B:CYS145 4.6 76.5 1.0 CB B:CYS155 4.6 79.2 1.0 N B:PRO144 4.6 56.7 1.0 N B:CYS154 4.7 59.8 1.0 CA B:CYS155 4.7 75.2 1.0 CA B:GLY164 4.7 64.2 1.0 O B:HIS143 4.7 76.2 1.0 CB B:GLN166 4.8 46.2 1.0 N B:CYS145 4.9 59.3 1.0

E.Baraldi, K.Djinovic Carugo, M.Hyvonen, P.L.Surdo, A.M.Riley, B.V.Potter, R.O'brien, J.E.Ladbury, M.Saraste. Structure of the pH Domain From Bruton'S Tyrosine Kinase in Complex with Inositol 1,3,4,5-Tetrakisphosphate. Structure Fold.Des. V. 7 449 1999.
ISSN: ISSN 0969-2126
PubMed: 10196129
DOI: 10.1016/S0969-2126(99)80057-4