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Iron in PDB 2evk: The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models For Cytochrome P450 and For Oxyanion-Bound Heme Proteins

Protein crystallography data

The structure of The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models For Cytochrome P450 and For Oxyanion-Bound Heme Proteins, PDB code: 2evk was solved by J.Qin, R.Perera, L.L.Lovelace, J.H.Dawson, L.Lebioda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.720, 47.995, 77.611, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26.4

Iron Binding Sites:

The binding sites of Iron atom in the The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models For Cytochrome P450 and For Oxyanion-Bound Heme Proteins (pdb code 2evk). 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 Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models For Cytochrome P450 and For Oxyanion-Bound Heme Proteins, PDB code: 2evk:

Iron binding site 1 out of 1 in 2evk

Go back to Iron Binding Sites List in 2evk
Iron binding site 1 out of 1 in the The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models For Cytochrome P450 and For Oxyanion-Bound Heme Proteins


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models For Cytochrome P450 and For Oxyanion-Bound Heme Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:15.1
occ:1.00
FE A:HEM154 0.0 15.1 1.0
ND A:HEM154 2.0 17.3 1.0
NA A:HEM154 2.1 15.2 1.0
NC A:HEM154 2.1 14.7 1.0
NB A:HEM154 2.1 13.8 1.0
OXT A:ACY155 2.2 18.6 1.0
O A:HOH1900 2.3 19.9 1.0
C4D A:HEM154 3.0 16.9 1.0
C1D A:HEM154 3.1 13.2 1.0
C1A A:HEM154 3.1 11.8 1.0
C4C A:HEM154 3.1 12.1 1.0
C4B A:HEM154 3.1 10.6 1.0
C4A A:HEM154 3.1 10.9 1.0
C1C A:HEM154 3.1 11.2 1.0
C1B A:HEM154 3.1 9.7 1.0
C A:ACY155 3.3 37.8 1.0
CHA A:HEM154 3.4 14.7 1.0
CHB A:HEM154 3.4 8.9 1.0
CHD A:HEM154 3.5 14.7 1.0
CHC A:HEM154 3.5 11.7 1.0
CH3 A:ACY155 4.1 24.2 1.0
C3D A:HEM154 4.3 16.6 1.0
C2D A:HEM154 4.3 18.2 1.0
C3B A:HEM154 4.3 10.1 1.0
C2A A:HEM154 4.3 13.9 1.0
C2B A:HEM154 4.3 12.2 1.0
C3A A:HEM154 4.3 13.2 1.0
C3C A:HEM154 4.3 16.8 1.0
C2C A:HEM154 4.4 14.8 1.0
O A:ACY155 4.4 37.6 1.0
CE1 A:HIS64 4.5 13.6 1.0
NE2 A:HIS64 4.5 19.8 1.0
CG2 A:VAL68 4.5 11.9 1.0

Reference:

J.Qin, R.Perera, L.L.Lovelace, J.H.Dawson, L.Lebioda. Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models For Cytochrome P450 and For Oxyanion-Bound Heme Proteins. Biochemistry V. 45 3170 2006.
ISSN: ISSN 0006-2960
PubMed: 16519512
DOI: 10.1021/BI052171S
Page generated: Sun Dec 13 14:43:47 2020

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