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Iron in PDB 1sy2: 1.0 A Crystal Structure of D129A/L130A Mutant of Nitrophorin 4

Protein crystallography data

The structure of 1.0 A Crystal Structure of D129A/L130A Mutant of Nitrophorin 4, PDB code: 1sy2 was solved by E.M.Maes, A.Weichsel, J.F.Andersen, D.Shepley, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.40 / 1.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.149, 42.804, 52.881, 90.00, 93.93, 90.00
R / Rfree (%) 15.6 / 17

Iron Binding Sites:

The binding sites of Iron atom in the 1.0 A Crystal Structure of D129A/L130A Mutant of Nitrophorin 4 (pdb code 1sy2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the 1.0 A Crystal Structure of D129A/L130A Mutant of Nitrophorin 4, PDB code: 1sy2:

Iron binding site 1 out of 1 in 1sy2

Go back to Iron Binding Sites List in 1sy2
Iron binding site 1 out of 1 in the 1.0 A Crystal Structure of D129A/L130A Mutant of Nitrophorin 4


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.0 A Crystal Structure of D129A/L130A Mutant of Nitrophorin 4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe185

b:7.1
occ:1.00
FE A:HEM185 0.0 7.1 1.0
NC A:HEM185 2.0 7.4 1.0
NE2 A:HIS59 2.0 6.7 1.0
NB A:HEM185 2.0 7.2 1.0
NA A:HEM185 2.0 7.3 1.0
N A:NH4200 2.0 9.2 1.0
ND A:HEM185 2.0 8.2 1.0
CE1 A:HIS59 3.0 6.3 1.0
C4C A:HEM185 3.0 8.3 1.0
CD2 A:HIS59 3.0 6.5 1.0
C1C A:HEM185 3.0 8.0 1.0
C4B A:HEM185 3.0 7.5 1.0
C4A A:HEM185 3.0 7.6 1.0
C1B A:HEM185 3.0 7.6 1.0
C1D A:HEM185 3.0 9.2 1.0
C1A A:HEM185 3.0 7.7 1.0
C4D A:HEM185 3.0 8.3 1.0
CHD A:HEM185 3.4 9.6 1.0
CHB A:HEM185 3.4 8.1 1.0
CHC A:HEM185 3.4 8.2 1.0
CHA A:HEM185 3.4 8.2 1.0
ND1 A:HIS59 4.1 5.8 1.0
CG A:HIS59 4.1 6.1 1.0
C3C A:HEM185 4.2 9.7 1.0
C2C A:HEM185 4.2 9.2 1.0
C3A A:HEM185 4.2 8.1 1.0
C3B A:HEM185 4.2 8.3 1.0
C2B A:HEM185 4.2 8.0 1.0
C2A A:HEM185 4.3 8.0 1.0
C2D A:HEM185 4.3 10.9 1.0
C3D A:HEM185 4.3 10.2 1.0
O A:HOH238 4.7 20.4 1.0
CD2 A:LEU133 4.8 13.0 1.0

Reference:

E.M.Maes, A.Weichsel, J.F.Andersen, D.Shepley, W.R.Montfort. Role of Binding Site Loops in Controlling Nitric Oxide Release: Structure and Kinetics of Mutant Forms of Nitrophorin 4 Biochemistry V. 43 6679 2004.
ISSN: ISSN 0006-2960
PubMed: 15157102
DOI: 10.1021/BI049748A
Page generated: Sat Aug 3 15:04:44 2024

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