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Iron in PDB 6rp5: Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus

Protein crystallography data

The structure of Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus, PDB code: 6rp5 was solved by N.Balasco, L.Vitagliano, A.Merlino, C.Verde, L.Mazzarella, A.Vergara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.42 / 1.49
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 91.702, 91.702, 168.716, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 19.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus (pdb code 6rp5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus, PDB code: 6rp5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 6rp5

Go back to Iron Binding Sites List in 6rp5
Iron binding site 1 out of 2 in the Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:24.7
occ:1.00
FE A:HEM202 0.0 24.7 1.0
C A:CMO201 1.8 26.7 1.0
ND A:HEM202 1.9 24.6 1.0
NB A:HEM202 2.0 24.9 1.0
NA A:HEM202 2.0 23.1 1.0
NC A:HEM202 2.1 22.1 1.0
NE2 A:HIS88 2.1 26.2 1.0
O A:CMO201 2.9 29.3 1.0
C4D A:HEM202 3.0 24.6 1.0
C4B A:HEM202 3.0 23.9 1.0
C1C A:HEM202 3.0 23.6 1.0
C1A A:HEM202 3.0 24.0 1.0
C1D A:HEM202 3.0 22.1 1.0
C4A A:HEM202 3.1 25.0 1.0
CE1 A:HIS88 3.1 28.0 1.0
C1B A:HEM202 3.1 26.8 1.0
C4C A:HEM202 3.1 22.4 1.0
CD2 A:HIS88 3.1 24.3 1.0
CHC A:HEM202 3.3 24.1 1.0
CHB A:HEM202 3.4 26.2 1.0
CHD A:HEM202 3.4 23.1 1.0
CHA A:HEM202 3.4 26.4 1.0
ND1 A:HIS88 4.2 25.1 1.0
C3A A:HEM202 4.2 25.9 1.0
C2A A:HEM202 4.2 27.0 1.0
C3C A:HEM202 4.2 22.5 1.0
C2C A:HEM202 4.2 25.3 1.0
C2D A:HEM202 4.3 24.9 1.0
CG A:HIS88 4.3 24.5 1.0
C2B A:HEM202 4.3 27.5 1.0
C3D A:HEM202 4.3 26.3 1.0
C3B A:HEM202 4.3 27.9 1.0

Iron binding site 2 out of 2 in 6rp5

Go back to Iron Binding Sites List in 6rp5
Iron binding site 2 out of 2 in the Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Monocarboxylated Hemoglobin From the Sub- Antarctic Fish Eleginops Maclovinus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:29.1
occ:1.00
FE B:HEM202 0.0 29.1 1.0
C B:CMO201 1.8 29.7 1.0
ND B:HEM202 2.0 31.0 1.0
NA B:HEM202 2.0 31.4 1.0
NC B:HEM202 2.0 25.7 1.0
NB B:HEM202 2.1 28.6 1.0
NE2 B:HIS92 2.2 29.4 1.0
O B:CMO201 3.0 33.1 1.0
C1A B:HEM202 3.0 30.4 1.0
C4D B:HEM202 3.0 31.2 1.0
C1D B:HEM202 3.0 27.8 1.0
C1C B:HEM202 3.0 26.3 1.0
C4A B:HEM202 3.0 32.1 1.0
C4B B:HEM202 3.0 25.9 1.0
C4C B:HEM202 3.0 28.5 1.0
CE1 B:HIS92 3.1 29.8 1.0
C1B B:HEM202 3.1 30.3 1.0
CD2 B:HIS92 3.2 26.6 1.0
CHC B:HEM202 3.4 27.9 1.0
CHA B:HEM202 3.4 31.3 1.0
CHD B:HEM202 3.4 27.7 1.0
CHB B:HEM202 3.4 30.6 1.0
C3A B:HEM202 4.2 34.1 1.0
C2A B:HEM202 4.2 32.6 1.0
ND1 B:HIS92 4.2 30.4 1.0
C3C B:HEM202 4.2 25.9 1.0
C2C B:HEM202 4.2 25.9 1.0
C2D B:HEM202 4.3 31.8 1.0
C3D B:HEM202 4.3 32.2 1.0
CG B:HIS92 4.3 28.8 1.0
C2B B:HEM202 4.3 30.4 1.0
C3B B:HEM202 4.3 28.7 1.0
CG2 B:VAL67 4.6 30.0 1.0

Reference:

N.Balasco, L.Vitagliano, A.Merlino, C.Verde, L.Mazzarella, A.Vergara. The Unique Structural Features of Carbonmonoxy Hemoglobin From the Sub-Antarctic Fish Eleginops Maclovinus. Sci Rep V. 9 18987 2019.
ISSN: ESSN 2045-2322
PubMed: 31831781
DOI: 10.1038/S41598-019-55331-3
Page generated: Wed Aug 7 08:52:39 2024

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