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Iron in PDB 1xch: Myoglobin (Horse Heart) Mutant with Leu 104 Replaced By Asn (L104N)

Protein crystallography data

The structure of Myoglobin (Horse Heart) Mutant with Leu 104 Replaced By Asn (L104N), PDB code: 1xch was solved by R.Maurus, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.566, 28.872, 35.882, 90.00, 107.17, 90.00
R / Rfree (%) 17.9 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Myoglobin (Horse Heart) Mutant with Leu 104 Replaced By Asn (L104N) (pdb code 1xch). 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 Myoglobin (Horse Heart) Mutant with Leu 104 Replaced By Asn (L104N), PDB code: 1xch:

Iron binding site 1 out of 1 in 1xch

Go back to Iron Binding Sites List in 1xch
Iron binding site 1 out of 1 in the Myoglobin (Horse Heart) Mutant with Leu 104 Replaced By Asn (L104N)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Myoglobin (Horse Heart) Mutant with Leu 104 Replaced By Asn (L104N) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:12.6
occ:1.00
FE A:HEM154 0.0 12.6 1.0
NB A:HEM154 2.0 11.2 1.0
NA A:HEM154 2.0 9.7 1.0
ND A:HEM154 2.0 11.6 1.0
NC A:HEM154 2.0 10.3 1.0
NE2 A:HIS93 2.1 8.5 1.0
O A:HOH156 2.3 13.0 1.0
C4A A:HEM154 3.0 8.8 1.0
C4B A:HEM154 3.0 10.3 1.0
C4C A:HEM154 3.0 8.7 1.0
C1C A:HEM154 3.1 7.8 1.0
C4D A:HEM154 3.1 9.7 1.0
C1B A:HEM154 3.1 9.8 1.0
C1A A:HEM154 3.1 8.6 1.0
CD2 A:HIS93 3.1 11.9 1.0
C1D A:HEM154 3.1 10.8 1.0
CE1 A:HIS93 3.1 13.7 1.0
CHC A:HEM154 3.4 10.9 1.0
CHB A:HEM154 3.4 9.1 1.0
CHD A:HEM154 3.4 8.9 1.0
CHA A:HEM154 3.4 9.6 1.0
ND1 A:HIS93 4.2 13.4 1.0
CG A:HIS93 4.2 10.8 1.0
C3A A:HEM154 4.3 7.8 1.0
C2A A:HEM154 4.3 7.2 1.0
C3B A:HEM154 4.3 11.7 1.0
C2C A:HEM154 4.3 10.3 1.0
C3C A:HEM154 4.3 9.7 1.0
C2B A:HEM154 4.3 9.5 1.0
C3D A:HEM154 4.3 12.5 1.0
C2D A:HEM154 4.3 11.8 1.0
NE2 A:HIS64 4.5 12.6 1.0
CG2 A:VAL68 4.8 10.8 1.0
CE1 A:HIS64 4.9 14.6 1.0

Reference:

R.Maurus, C.M.Overall, R.Bogumil, Y.Luo, A.G.Mauk, M.Smith, G.D.Brayer. A Myoglobin Variant with A Polar Substitution in A Conserved Hydrophobic Cluster in the Heme Binding Pocket. Biochim.Biophys.Acta V.1341 1 1997.
ISSN: ISSN 0006-3002
PubMed: 9300804
DOI: 10.1016/S0167-4838(97)00064-2
Page generated: Sun Dec 13 14:35:44 2020

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