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Iron in PDB 5jom: X-Ray Structure of Co-Bound Sperm Whale Myoglobin Using A Fixed Target Crystallography Chip

Protein crystallography data

The structure of X-Ray Structure of Co-Bound Sperm Whale Myoglobin Using A Fixed Target Crystallography Chip, PDB code: 5jom was solved by S.Oghbaey, A.Sarracini, H.M.Ginn, O.Pare-Labrosse, A.Kuo, A.Marx, S.W.Epp, D.A.Sherrell, B.T.Eger, Y.Zhong, R.Loch, V.Mariani, R.Alonso-Mori, S.Nelson, H.T.Lemke, R.L.Owen, A.R.Pearson, D.I.Stuart, O.P.Ernst, H.M.Mueller-Werkmeister, R.J.D.Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.43 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.130, 46.483, 84.521, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 25.9

Iron Binding Sites:

The binding sites of Iron atom in the X-Ray Structure of Co-Bound Sperm Whale Myoglobin Using A Fixed Target Crystallography Chip (pdb code 5jom). 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 X-Ray Structure of Co-Bound Sperm Whale Myoglobin Using A Fixed Target Crystallography Chip, PDB code: 5jom:

Iron binding site 1 out of 1 in 5jom

Go back to Iron Binding Sites List in 5jom
Iron binding site 1 out of 1 in the X-Ray Structure of Co-Bound Sperm Whale Myoglobin Using A Fixed Target Crystallography Chip


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Structure of Co-Bound Sperm Whale Myoglobin Using A Fixed Target Crystallography Chip within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:30.9
occ:1.00
FE A:HEM201 0.0 30.9 1.0
ND A:HEM201 1.9 32.8 1.0
C A:CMO203 2.0 23.4 1.0
NA A:HEM201 2.0 31.4 1.0
NB A:HEM201 2.1 29.8 1.0
NE2 A:HIS93 2.1 34.2 1.0
NC A:HEM201 2.1 27.5 1.0
C1D A:HEM201 2.9 30.9 1.0
C4D A:HEM201 2.9 35.2 1.0
CE1 A:HIS93 3.0 36.0 1.0
C1A A:HEM201 3.0 34.6 1.0
C4A A:HEM201 3.0 30.8 1.0
C1B A:HEM201 3.0 28.2 1.0
C4B A:HEM201 3.0 31.3 1.0
O A:CMO203 3.1 36.3 1.0
C4C A:HEM201 3.1 30.0 1.0
C1C A:HEM201 3.1 28.7 1.0
CD2 A:HIS93 3.1 33.4 1.0
CHB A:HEM201 3.4 27.5 1.0
CHA A:HEM201 3.4 35.0 1.0
CHD A:HEM201 3.4 32.2 1.0
CHC A:HEM201 3.5 29.7 1.0
ND1 A:HIS93 4.1 38.9 1.0
C2D A:HEM201 4.2 32.4 1.0
C2A A:HEM201 4.2 34.0 1.0
C3A A:HEM201 4.2 31.5 1.0
C3D A:HEM201 4.2 34.2 1.0
CG A:HIS93 4.2 32.5 1.0
C2B A:HEM201 4.3 30.1 1.0
C3B A:HEM201 4.3 31.8 1.0
C2C A:HEM201 4.3 26.5 1.0
C3C A:HEM201 4.3 29.4 1.0
NE2 A:HIS64 4.6 36.5 1.0
CG2 A:VAL68 4.7 31.0 1.0

Reference:

S.Oghbaey, A.Sarracini, H.M.Ginn, O.Pare-Labrosse, A.Kuo, A.Marx, S.W.Epp, D.A.Sherrell, B.T.Eger, Y.Zhong, R.Loch, V.Mariani, R.Alonso-Mori, S.Nelson, H.T.Lemke, R.L.Owen, A.R.Pearson, D.I.Stuart, O.P.Ernst, H.M.Mueller-Werkmeister, R.J.Miller. Fixed Target Combined with Spectral Mapping: Approaching 100% Hit Rates For Serial Crystallography. Acta Crystallogr D Struct V. 72 944 2016BIOL.
ISSN: ISSN 2059-7983
PubMed: 27487825
DOI: 10.1107/S2059798316010834
Page generated: Tue Aug 6 02:34:34 2024

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