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Zinc in PDB 4mlt: Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii

Enzymatic activity of Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii

All present enzymatic activity of Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii:
4.2.1.1;

Protein crystallography data

The structure of Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii, PDB code: 4mlt was solved by D.P.Martin, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.145, 41.472, 72.029, 90.00, 104.19, 90.00
R / Rfree (%) 17.2 / 24.1

Other elements in 4mlt:

The structure of Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii (pdb code 4mlt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii, PDB code: 4mlt:

Zinc binding site 1 out of 1 in 4mlt

Go back to Zinc Binding Sites List in 4mlt
Zinc binding site 1 out of 1 in the Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of A Monodentate 3-Hydroxy-4H-Pyran-4-Thione Ligand Bound to Hcaii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:8.7
occ:1.00
 NE2 A:HIS96 2.0 4.8 1.0
ND1 A:HIS119 2.0 5.1 1.0
NE2 A:HIS94 2.1 7.7 1.0
S1 A:TM4303 2.4 38.4 1.0
CE1 A:HIS119 2.9 3.7 1.0
CE1 A:HIS96 2.9 7.5 1.0
CD2 A:HIS94 3.0 2.5 1.0
CD2 A:HIS96 3.1 4.2 1.0
CE1 A:HIS94 3.1 9.9 1.0
CG A:HIS119 3.1 2.0 1.0
C3 A:TM4303 3.4 41.1 0.5
C3 A:TM4303 3.5 41.5 0.5
CB A:HIS119 3.6 2.0 1.0
C4 A:TM4303 3.8 40.9 0.5
OG1 A:THR199 3.8 2.0 1.0
O2 A:TM4303 3.8 40.4 0.5
OE1 A:GLU106 4.0 11.7 1.0
NE2 A:HIS119 4.1 3.6 1.0
C2 A:TM4303 4.1 41.2 0.5
ND1 A:HIS96 4.1 2.1 1.0
CG A:HIS94 4.1 5.8 1.0
ND1 A:HIS94 4.2 7.4 1.0
CG A:HIS96 4.2 2.0 1.0
CD2 A:HIS119 4.2 3.9 1.0
C2 A:TM4303 4.4 40.0 0.5
C4 A:TM4303 4.5 41.1 0.5
O2 A:TM4303 4.8 40.5 0.5
C5 A:TM4303 4.9 41.2 0.5
CD A:GLU106 4.9 5.4 1.0

Reference:

D.P.Martin, P.G.Blachly, A.R.Marts, T.M.Woodruff, C.A.De Oliveira, J.A.Mccammon, D.L.Tierney, S.M.Cohen. 'Unconventional' Coordination Chemistry By Metal Chelating Fragments in A Metalloprotein Active Site. J.Am.Chem.Soc. V. 136 5400 2014.
ISSN: ISSN 0002-7863
PubMed: 24635441
DOI: 10.1021/JA500616M
Page generated: Sun Oct 27 02:34:02 2024

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