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Zinc in PDB 9j9l: Artificial Mononuclear Zn-Bound Metalloprotein 1 (M1:Zn)

Protein crystallography data

The structure of Artificial Mononuclear Zn-Bound Metalloprotein 1 (M1:Zn), PDB code: 9j9l was solved by W.J.Jeong, W.J.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.66 / 2.60
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 136.99, 136.99, 49.66, 90, 90, 120
R / Rfree (%) 19.5 / 27.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Artificial Mononuclear Zn-Bound Metalloprotein 1 (M1:Zn) (pdb code 9j9l). 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 Artificial Mononuclear Zn-Bound Metalloprotein 1 (M1:Zn), PDB code: 9j9l:

Zinc binding site 1 out of 1 in 9j9l

Go back to Zinc Binding Sites List in 9j9l
Zinc binding site 1 out of 1 in the Artificial Mononuclear Zn-Bound Metalloprotein 1 (M1:Zn)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Artificial Mononuclear Zn-Bound Metalloprotein 1 (M1:Zn) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:46.6
occ:1.00
NE2 A:HIS102 2.0 48.8 1.0
OD1 A:ASP132 2.1 46.6 1.0
N1 A:BCN402 2.2 56.7 1.0
NE2 A:HIS82 2.3 54.5 1.0
C4 A:BCN402 2.6 47.8 1.0
C6 A:BCN402 2.6 66.3 1.0
C3 A:BCN402 2.8 50.0 1.0
CD2 A:HIS102 3.0 51.4 1.0
C5 A:BCN402 3.0 55.8 1.0
CE1 A:HIS102 3.0 48.4 1.0
CD2 A:HIS82 3.1 48.8 1.0
C1 A:BCN402 3.1 59.9 1.0
CG A:ASP132 3.2 48.0 1.0
CE1 A:HIS82 3.4 51.7 1.0
OD2 A:ASP132 3.7 57.2 1.0
O6 A:BCN402 3.7 77.6 1.0
O4 A:BCN402 3.8 53.2 1.0
CG A:HIS102 4.1 43.3 1.0
ND1 A:HIS102 4.1 45.9 1.0
CG A:HIS82 4.2 52.9 1.0
C2 A:BCN402 4.3 79.5 1.0
ND1 A:HIS82 4.4 52.2 1.0
CB A:ASP132 4.5 48.2 1.0
O21 A:BCN402 4.6 78.9 1.0
CD2 A:LEU83 4.7 56.4 1.0
N A:ASP132 4.9 42.9 1.0
CA A:ASP132 5.0 48.0 1.0

Reference:

W.J.Jeong, W.J.Song. Metal-Installer: A Protein Designer Tool to Create Metal-Binding Sites To Be Published.
Page generated: Fri Aug 22 18:20:28 2025

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