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Zinc in PDB 4nef: X-Ray Structure of Human Aquaporin 2

Protein crystallography data

The structure of X-Ray Structure of Human Aquaporin 2, PDB code: 4nef was solved by A.Frick, U.Eriksson, F.D.Mattia, F.Oberg, K.Hedfalk, R.Neutze, W.D.Grip, P.M.T.Deen, S.Tornroth-Horsefield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.96 / 2.75
Space group P 42
Cell size a, b, c (Å), α, β, γ (°) 119.110, 119.110, 90.621, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 22.5

Other elements in 4nef:

The structure of X-Ray Structure of Human Aquaporin 2 also contains other interesting chemical elements:

Cadmium (Cd) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Structure of Human Aquaporin 2 (pdb code 4nef). 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 X-Ray Structure of Human Aquaporin 2, PDB code: 4nef:

Zinc binding site 1 out of 1 in 4nef

Go back to Zinc Binding Sites List in 4nef
Zinc binding site 1 out of 1 in the X-Ray Structure of Human Aquaporin 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of Human Aquaporin 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:77.5
occ:0.51
SG A:CYS75 2.3 81.2 1.0
O A:HOH413 2.5 54.4 1.0
ND1 A:HIS80 2.8 0.4 1.0
CG A:HIS80 3.0 0.2 1.0
CB A:HIS80 3.2 99.6 1.0
CB A:CYS75 3.4 79.8 1.0
O A:HOH403 3.6 76.5 1.0
CE1 A:HIS80 3.6 0.4 1.0
CD2 A:HIS80 3.9 0.3 1.0
CA A:CYS75 4.0 80.1 1.0
NE2 A:HIS80 4.2 1.0 1.0
CE1 A:PHE146 4.4 74.7 1.0
CZ A:PHE146 4.5 75.0 1.0
CA A:HIS80 4.7 0.3 1.0
CE1 A:HIS66 4.8 77.4 1.0
O A:CYS75 4.9 86.9 1.0
C A:CYS75 5.0 87.4 1.0

Reference:

A.Frick, U.Eriksson, F.D.Mattia, F.Oberg, K.Hedfalk, R.Neutze, W.D.Grip, P.M.T.Deen, S.Tornroth-Horsefield. X-Ray Structure of Human Aquapor in 2 and Its Implications For Nephrogenic Diabetes Insipidus and Trafficking Proc.Natl.Acad.Sci.Usa 2014.
ISSN: ESSN 1091-6490
Page generated: Wed Dec 16 05:36:59 2020

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