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Iron in PDB 1mnk: Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin

Protein crystallography data

The structure of Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin, PDB code: 1mnk was solved by S.Krzywda, A.J.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.20
Space group I 21
Cell size a, b, c (Å), α, β, γ (°) 125.260, 42.490, 92.370, 90.00, 92.29, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin (pdb code 1mnk). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin, PDB code: 1mnk:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1mnk

Go back to Iron Binding Sites List in 1mnk
Iron binding site 1 out of 2 in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:18.4
occ:1.00
FE A:HEM154 0.0 18.4 1.0
NC A:HEM154 2.0 17.9 1.0
NA A:HEM154 2.0 18.5 1.0
ND A:HEM154 2.0 19.7 1.0
NB A:HEM154 2.1 17.1 1.0
NE2 A:HIS93 2.2 18.7 1.0
O A:HOH157 2.2 16.1 1.0
C4C A:HEM154 3.0 18.3 1.0
C1A A:HEM154 3.0 19.5 1.0
C4A A:HEM154 3.1 18.4 1.0
C1C A:HEM154 3.1 17.8 1.0
C4D A:HEM154 3.1 20.0 1.0
C1D A:HEM154 3.1 19.6 1.0
CE1 A:HIS93 3.1 18.8 1.0
C4B A:HEM154 3.1 16.4 1.0
C1B A:HEM154 3.1 16.1 1.0
CD2 A:HIS93 3.2 14.0 1.0
CHA A:HEM154 3.4 19.3 1.0
CHD A:HEM154 3.4 18.7 1.0
CHC A:HEM154 3.5 16.7 1.0
CHB A:HEM154 3.5 16.6 1.0
ND1 A:HIS93 4.2 16.4 1.0
C3C A:HEM154 4.2 18.5 1.0
C2A A:HEM154 4.3 19.5 1.0
C2C A:HEM154 4.3 17.6 1.0
C3D A:HEM154 4.3 21.1 1.0
C3A A:HEM154 4.3 18.6 1.0
C3B A:HEM154 4.3 16.1 1.0
CG A:HIS93 4.3 17.0 1.0
C2B A:HEM154 4.3 15.9 1.0
C2D A:HEM154 4.3 20.6 1.0
OG1 A:THR68 4.7 11.6 1.0

Iron binding site 2 out of 2 in 1mnk

Go back to Iron Binding Sites List in 1mnk
Iron binding site 2 out of 2 in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe154

b:19.1
occ:1.00
FE B:HEM154 0.0 19.1 1.0
NC B:HEM154 2.0 17.5 1.0
NA B:HEM154 2.0 18.3 1.0
ND B:HEM154 2.0 19.2 1.0
NB B:HEM154 2.0 16.5 1.0
NE2 B:HIS93 2.1 19.7 1.0
O B:HOH155 2.4 18.1 1.0
CE1 B:HIS93 3.0 19.6 1.0
C4C B:HEM154 3.0 17.7 1.0
C1D B:HEM154 3.0 19.4 1.0
C1C B:HEM154 3.0 17.5 1.0
C4A B:HEM154 3.0 17.9 1.0
C1A B:HEM154 3.1 19.2 1.0
C4D B:HEM154 3.1 19.8 1.0
C1B B:HEM154 3.1 15.3 1.0
C4B B:HEM154 3.1 15.8 1.0
CD2 B:HIS93 3.2 18.4 1.0
CHD B:HEM154 3.4 18.4 1.0
CHB B:HEM154 3.4 15.7 1.0
CHC B:HEM154 3.5 16.4 1.0
CHA B:HEM154 3.5 19.3 1.0
ND1 B:HIS93 4.2 19.1 1.0
C3D B:HEM154 4.2 21.1 1.0
C3C B:HEM154 4.2 17.5 1.0
C2A B:HEM154 4.3 19.3 1.0
C2C B:HEM154 4.3 17.2 1.0
C2D B:HEM154 4.3 20.4 1.0
C3A B:HEM154 4.3 18.3 1.0
CG B:HIS93 4.3 22.7 1.0
C2B B:HEM154 4.3 14.7 1.0
C3B B:HEM154 4.3 14.7 1.0
O B:HOH255 4.5 47.5 0.0
OG1 B:THR68 4.7 11.9 1.0

Reference:

S.J.Smerdon, S.Krzywda, A.M.Brzozowski, G.J.Davies, A.J.Wilkinson, A.Brancaccio, F.Cutruzzola, C.T.Allocatelli, M.Brunori, T.Li, R.E.Brantley Jr., T.E.Carver, R.F.Eich, E.Singleton, J.S.Olson. Interactions Among Residues CD3, E7, E10, and E11 in Myoglobins: Attempts to Simulate the Ligand-Binding Properties of Aplysia Myoglobin. Biochemistry V. 34 8715 1995.
ISSN: ISSN 0006-2960
PubMed: 7612611
DOI: 10.1021/BI00027A022
Page generated: Wed Jul 16 18:15:55 2025

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