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Zinc in PDB 3m3b: The Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin: Zn(II)-I107E Febmb (Zn(II) Binding to Feb Site)

Protein crystallography data

The structure of The Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin: Zn(II)-I107E Febmb (Zn(II) Binding to Feb Site), PDB code: 3m3b was solved by Y.-W.Lin, N.Yeung, Y.-G.Gao, K.D.Miner, S.Tian, H.Robinson, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.760, 47.540, 77.210, 90.00, 90.00, 90.00
R / Rfree (%) n/a / 26.1

Other elements in 3m3b:

The structure of The Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin: Zn(II)-I107E Febmb (Zn(II) Binding to Feb Site) also contains other interesting chemical elements:

Iron (Fe) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the The Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin: Zn(II)-I107E Febmb (Zn(II) Binding to Feb Site) (pdb code 3m3b). 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 The Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin: Zn(II)-I107E Febmb (Zn(II) Binding to Feb Site), PDB code: 3m3b:

Zinc binding site 1 out of 1 in 3m3b

Go back to Zinc Binding Sites List in 3m3b
Zinc binding site 1 out of 1 in the The Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin: Zn(II)-I107E Febmb (Zn(II) Binding to Feb Site)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin: Zn(II)-I107E Febmb (Zn(II) Binding to Feb Site) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn156

b:32.3
occ:1.00
NE2 A:HIS29 2.1 23.2 1.0
NE2 A:HIS64 2.1 24.5 1.0
NE2 A:HIS43 2.2 47.0 1.0
OE1 A:GLU68 2.3 28.2 1.0
OE2 A:GLU68 2.3 23.7 1.0
CD A:GLU68 2.6 25.8 1.0
CD2 A:HIS64 2.9 17.1 1.0
CE1 A:HIS29 3.0 30.1 1.0
CD2 A:HIS43 3.1 46.8 1.0
CD2 A:HIS29 3.1 27.1 1.0
CE1 A:HIS64 3.2 22.9 1.0
CE1 A:HIS43 3.2 38.8 1.0
CG A:GLU68 4.0 23.1 1.0
CG A:HIS64 4.1 15.3 1.0
ND1 A:HIS64 4.2 18.8 1.0
ND1 A:HIS29 4.2 31.6 1.0
CG A:HIS29 4.2 21.8 1.0
CG A:HIS43 4.3 40.1 1.0
C4C A:HEM155 4.3 20.1 1.0
ND1 A:HIS43 4.3 33.3 1.0
NC A:HEM155 4.3 22.0 1.0
OE2 A:GLU107 4.5 43.7 1.0
C3C A:HEM155 4.5 20.4 1.0
CHD A:HEM155 4.6 20.8 1.0
OE1 A:GLU107 4.6 50.6 1.0
C1C A:HEM155 4.6 17.9 1.0
FE A:HEM155 4.8 16.8 1.0
C1D A:HEM155 4.8 20.1 1.0
ND A:HEM155 4.8 19.4 1.0
C2C A:HEM155 4.9 16.9 1.0
CB A:GLU68 4.9 18.0 1.0

Reference:

Y.W.Lin, N.Yeung, Y.G.Gao, K.D.Miner, S.Tian, H.Robinson, Y.Lu. Roles of Glutamates and Metal Ions in A Rationally Designed Nitric Oxide Reductase Based on Myoglobin. Proc.Natl.Acad.Sci.Usa V. 107 8581 2010.
ISSN: ISSN 0027-8424
PubMed: 20421510
DOI: 10.1073/PNAS.1000526107
Page generated: Sat Oct 26 09:05:14 2024

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