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Zinc in PDB 4rdr: Structure of the Bacterial Zn-Transporter Znud From Neisseria Meningitidis (Locked Conformation Bound to Zinc and Cadmium Ions)

Protein crystallography data

The structure of Structure of the Bacterial Zn-Transporter Znud From Neisseria Meningitidis (Locked Conformation Bound to Zinc and Cadmium Ions), PDB code: 4rdr was solved by C.Calmettes, T.F.Moraes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.98 / 2.47
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 101.073, 155.819, 159.607, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 24.8

Other elements in 4rdr:

The structure of Structure of the Bacterial Zn-Transporter Znud From Neisseria Meningitidis (Locked Conformation Bound to Zinc and Cadmium Ions) also contains other interesting chemical elements:

Cadmium (Cd) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Bacterial Zn-Transporter Znud From Neisseria Meningitidis (Locked Conformation Bound to Zinc and Cadmium Ions) (pdb code 4rdr). 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 the Bacterial Zn-Transporter Znud From Neisseria Meningitidis (Locked Conformation Bound to Zinc and Cadmium Ions), PDB code: 4rdr:

Zinc binding site 1 out of 1 in 4rdr

Go back to Zinc Binding Sites List in 4rdr
Zinc binding site 1 out of 1 in the Structure of the Bacterial Zn-Transporter Znud From Neisseria Meningitidis (Locked Conformation Bound to Zinc and Cadmium Ions)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Bacterial Zn-Transporter Znud From Neisseria Meningitidis (Locked Conformation Bound to Zinc and Cadmium Ions) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn803

b:58.2
occ:1.00
OD2 A:ASP99 1.9 55.6 1.0
NE2 A:HIS499 2.0 78.2 1.0
OE2 A:GLU340 2.0 57.2 1.0
NE2 A:HIS100 2.1 62.0 1.0
CE1 A:HIS499 2.6 87.2 1.0
CG A:ASP99 2.9 66.8 1.0
CD2 A:HIS100 3.0 54.2 1.0
CD A:GLU340 3.0 62.3 1.0
CE1 A:HIS100 3.1 54.1 1.0
CD2 A:HIS499 3.2 79.8 1.0
CB A:ASP99 3.4 49.9 1.0
OE1 A:GLU340 3.4 62.8 1.0
OG A:SER97 3.5 82.5 1.0
ND1 A:HIS499 3.8 80.7 1.0
OD1 A:ASP99 3.9 91.7 1.0
CG A:HIS499 4.1 80.0 1.0
CG A:HIS100 4.1 59.2 1.0
CZ A:PHE350 4.1 66.7 1.0
ND1 A:HIS100 4.2 61.0 1.0
CE1 A:PHE350 4.2 68.6 1.0
CG A:GLU340 4.3 66.5 1.0
NE2 A:HIS338 4.4 59.6 1.0
CB A:ALA501 4.5 75.4 1.0
CB A:SER97 4.7 66.6 1.0
CD1 A:ILE304 4.8 58.4 1.0
CA A:ASP99 4.8 60.4 1.0
CE1 A:HIS338 4.8 62.2 1.0
CE2 A:PHE350 4.9 68.8 1.0
CD1 A:PHE350 5.0 64.1 1.0

Reference:

C.Calmettes, C.Ing, C.M.Buckwalter, M.El Bakkouri, C.Chieh-Lin Lai, A.Pogoutse, S.D.Gray-Owen, R.Pomes, T.F.Moraes. The Molecular Mechanism of Zinc Acquisition By the Neisserial Outer-Membrane Transporter Znud. Nat Commun V. 6 7996 2015.
ISSN: ESSN 2041-1723
PubMed: 26282243
DOI: 10.1038/NCOMMS8996
Page generated: Wed Dec 16 05:45:36 2020

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