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Iron in PDB 1iej: Ovotransferrin, N-Terminal Lobe, Holo Form, at 1.65 A Resolution

Protein crystallography data

The structure of Ovotransferrin, N-Terminal Lobe, Holo Form, at 1.65 A Resolution, PDB code: 1iej was solved by K.Mizutani, B.Mikami, M.Hirose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.460, 85.950, 76.100, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 24.2

Iron Binding Sites:

The binding sites of Iron atom in the Ovotransferrin, N-Terminal Lobe, Holo Form, at 1.65 A Resolution (pdb code 1iej). 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 Ovotransferrin, N-Terminal Lobe, Holo Form, at 1.65 A Resolution, PDB code: 1iej:

Iron binding site 1 out of 1 in 1iej

Go back to Iron Binding Sites List in 1iej
Iron binding site 1 out of 1 in the Ovotransferrin, N-Terminal Lobe, Holo Form, at 1.65 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ovotransferrin, N-Terminal Lobe, Holo Form, at 1.65 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe333

b:9.3
occ:1.00
OH A:TYR92 1.9 7.8 1.0
OH A:TYR191 2.0 7.8 1.0
O1 A:CO3334 2.1 4.5 1.0
O3 A:CO3334 2.1 6.4 1.0
NE2 A:HIS250 2.1 6.3 1.0
OD1 A:ASP60 2.1 8.4 1.0
C A:CO3334 2.4 6.6 1.0
CZ A:TYR92 3.0 4.2 1.0
CD2 A:HIS250 3.0 4.0 1.0
CZ A:TYR191 3.0 7.6 1.0
CE1 A:HIS250 3.1 4.2 1.0
CG A:ASP60 3.2 8.5 1.0
CE2 A:TYR92 3.6 4.7 1.0
O2 A:CO3334 3.6 7.8 1.0
CE1 A:TYR191 3.7 5.8 1.0
CB A:ASP60 3.8 6.8 1.0
O A:HOH378 4.0 7.6 1.0
CE2 A:TYR191 4.0 7.2 1.0
CE1 A:TYR92 4.0 3.6 1.0
OD2 A:ASP60 4.2 7.1 1.0
CG A:HIS250 4.2 4.2 1.0
ND1 A:HIS250 4.2 5.1 1.0
NZ A:LYS301 4.4 5.6 1.0
CA A:ASP60 4.5 6.1 1.0
CB A:SER122 4.5 6.5 1.0
NH2 A:ARG121 4.5 8.6 1.0
N A:SER122 4.8 5.7 1.0
OG A:SER122 4.8 8.0 1.0
N A:ALA123 4.8 6.4 1.0
NE A:ARG121 4.8 9.0 1.0
CD2 A:TYR92 4.9 6.2 1.0
CD A:LYS301 4.9 5.9 1.0
N A:GLY61 5.0 7.0 1.0

Reference:

K.Mizutani, B.Mikami, M.Hirose. Domain Closure Mechanism in Transferrins: New Viewpoints About the Hinge Structure and Motion As Deduced From High Resolution Crystal Structures of Ovotransferrin N-Lobe. J.Mol.Biol. V. 309 937 2001.
ISSN: ISSN 0022-2836
PubMed: 11399070
DOI: 10.1006/JMBI.2001.4719
Page generated: Sat Aug 3 08:04:24 2024

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