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Iron in PDB 1w92: The Structure of Carbomonoxy Murine Neuroglobin Reveals A Heme- Sliding Mechanism For Affinity Regulation

Protein crystallography data

The structure of The Structure of Carbomonoxy Murine Neuroglobin Reveals A Heme- Sliding Mechanism For Affinity Regulation, PDB code: 1w92 was solved by B.Vallone, K.Nienhaus, A.Matthes, M.Brunori, G.U.Nienhaus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 88.373, 88.373, 110.983, 90.00, 90.00, 120.00
R / Rfree (%) 26 / 22

Iron Binding Sites:

The binding sites of Iron atom in the The Structure of Carbomonoxy Murine Neuroglobin Reveals A Heme- Sliding Mechanism For Affinity Regulation (pdb code 1w92). 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 The Structure of Carbomonoxy Murine Neuroglobin Reveals A Heme- Sliding Mechanism For Affinity Regulation, PDB code: 1w92:

Iron binding site 1 out of 1 in 1w92

Go back to Iron Binding Sites List in 1w92
Iron binding site 1 out of 1 in the The Structure of Carbomonoxy Murine Neuroglobin Reveals A Heme- Sliding Mechanism For Affinity Regulation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Carbomonoxy Murine Neuroglobin Reveals A Heme- Sliding Mechanism For Affinity Regulation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1149

b:25.9
occ:1.00
FE A:HEM1149 0.0 25.9 1.0
C A:CMO1150 1.8 28.2 1.0
NC A:HEM1149 2.0 26.5 1.0
NA A:HEM1149 2.0 30.2 1.0
NB A:HEM1149 2.0 26.3 1.0
ND A:HEM1149 2.0 28.3 1.0
NE2 A:HIS96 2.1 35.6 1.0
O A:CMO1150 2.8 28.0 1.0
C4B A:HEM1149 3.0 27.9 1.0
C1C A:HEM1149 3.0 26.3 1.0
CD2 A:HIS96 3.0 37.4 1.0
C1A A:HEM1149 3.0 31.2 1.0
C4A A:HEM1149 3.0 29.9 1.0
C4D A:HEM1149 3.0 28.9 1.0
C4C A:HEM1149 3.0 26.9 1.0
C1D A:HEM1149 3.1 28.1 1.0
C1B A:HEM1149 3.1 27.3 1.0
CE1 A:HIS96 3.1 36.5 1.0
CHC A:HEM1149 3.4 26.7 1.0
CHD A:HEM1149 3.4 27.4 1.0
CHA A:HEM1149 3.4 30.9 1.0
CHB A:HEM1149 3.4 28.5 1.0
CG A:HIS96 4.2 38.5 1.0
ND1 A:HIS96 4.2 38.7 1.0
C3B A:HEM1149 4.2 27.5 1.0
C2C A:HEM1149 4.2 26.9 1.0
NE2 A:HIS64 4.2 19.1 1.0
C2A A:HEM1149 4.2 32.1 1.0
C3C A:HEM1149 4.3 27.3 1.0
C2B A:HEM1149 4.3 28.0 1.0
C3D A:HEM1149 4.3 28.9 1.0
C3A A:HEM1149 4.3 31.1 1.0
C2D A:HEM1149 4.3 28.5 1.0
CE1 A:HIS64 4.8 18.9 1.0
CG2 A:VAL68 5.0 17.5 1.0

Reference:

B.Vallone, K.Nienhaus, A.Matthes, M.Brunori, G.U.Nienhaus. The Structure of Carbonmonoxy Neuroglobin Reveals A Heme-Sliding Mechanism For Control of Ligand Affinity Proc.Natl.Acad.Sci.Usa V. 101 17351 2004.
ISSN: ISSN 0027-8424
PubMed: 15548613
DOI: 10.1073/PNAS.0407633101
Page generated: Wed Jul 16 21:48:29 2025

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