Zinc in PDB 1qiy: Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol

The structure of Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol, PDB code: 1qiy was solved by L.Tang, J.L.Whittingham, C.S.Verma, L.S.D.Caves, G.G.Dodson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.80 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.100, 62.080, 48.350, 90.00, 109.87, 90.00
R / Rfree (%)	18.6 / n/a

The structure of Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol (pdb code 1qiy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol, PDB code: 1qiy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn1001 b:19.0 occ:1.00 NE2 J:HIS10 2.1 23.2 1.0 NE2 B:HIS10 2.1 12.5 1.0 NE2 F:HIS10 2.1 20.1 1.0 CL J:CL1002 2.2 17.3 1.0 CE1 J:HIS10 3.0 11.9 1.0 CE1 B:HIS10 3.0 16.9 1.0 CE1 F:HIS10 3.1 14.3 1.0 CD2 J:HIS10 3.1 15.8 1.0 CD2 B:HIS10 3.2 10.3 1.0 CD2 F:HIS10 3.2 11.3 1.0 ND1 J:HIS10 4.1 11.2 1.0 ND1 B:HIS10 4.2 13.8 1.0 ND1 F:HIS10 4.2 19.3 1.0 CG J:HIS10 4.2 16.3 1.0 CG B:HIS10 4.3 18.0 1.0 CG F:HIS10 4.3 18.7 1.0 O F:LEU6 4.7 18.0 1.0 O B:LEU6 4.8 18.9 1.0 O J:LEU6 4.9 15.9 1.0 CB B:LEU6 4.9 15.9 1.0

Zinc binding site 2 out of 2 in the Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Insulin Hexamers with Chain B His Mutated to Tyr Complexed with Phenol within 5.0Å range: probe atom residue distance (Å) B Occ L:Zn1001 b:20.4 occ:1.00 NE2 L:HIS10 2.1 22.8 1.0 NE2 H:HIS10 2.1 23.4 1.0 NE2 D:HIS10 2.1 20.3 1.0 CL L:CL1002 2.2 19.1 1.0 CE1 L:HIS10 3.0 15.0 1.0 CE1 D:HIS10 3.0 14.5 1.0 CD2 L:HIS10 3.1 22.8 1.0 CE1 H:HIS10 3.1 19.0 1.0 CD2 H:HIS10 3.1 19.4 1.0 CD2 D:HIS10 3.2 14.2 1.0 ND1 L:HIS10 4.1 22.7 1.0 ND1 D:HIS10 4.2 21.1 1.0 CG L:HIS10 4.2 23.5 1.0 ND1 H:HIS10 4.2 18.7 1.0 CG H:HIS10 4.3 27.8 1.0 CG D:HIS10 4.3 17.9 1.0 O L:LEU6 4.9 19.9 1.0 O D:LEU6 4.9 22.3 1.0 O H:LEU6 4.9 21.8 1.0 CB L:LEU6 5.0 17.6 1.0

L.Tang, J.L.Whittingham, C.S.Verma, L.S.D.Caves, G.G.Dodson. Structural Consequences of the B5 Histidine --> Tyrosine Mutation in Human Insulin Characterized By X-Ray Crystallography and Conformational Analysis. Biochemistry V. 38 12041 1999.
ISSN: ISSN 0006-2960
PubMed: 10508408
DOI: 10.1021/BI990700K