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Iron in PDB 1oqg: Crystal Structure of the D63E Mutant of the N-Lobe Human Transferrin

Protein crystallography data

The structure of Crystal Structure of the D63E Mutant of the N-Lobe Human Transferrin, PDB code: 1oqg was solved by H.M.Baker, Q.-Y.He, S.K.Brigg, A.B.Mason, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.307, 57.312, 135.383, 90.00, 90.00, 90.00
R / Rfree (%) 24.5 / 26.1

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the D63E Mutant of the N-Lobe Human Transferrin (pdb code 1oqg). 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 Crystal Structure of the D63E Mutant of the N-Lobe Human Transferrin, PDB code: 1oqg:

Iron binding site 1 out of 1 in 1oqg

Go back to Iron Binding Sites List in 1oqg
Iron binding site 1 out of 1 in the Crystal Structure of the D63E Mutant of the N-Lobe Human Transferrin


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 the D63E Mutant of the N-Lobe Human Transferrin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:14.1
occ:1.00
OH A:TYR95 1.9 14.0 1.0
OH A:TYR188 2.0 12.2 1.0
OE2 A:GLU63 2.0 15.4 1.0
O3 A:CO3600 2.0 9.7 1.0
O2 A:CO3600 2.1 9.9 1.0
NE2 A:HIS249 2.2 14.1 1.0
C A:CO3600 2.4 9.9 1.0
CZ A:TYR95 3.0 14.1 1.0
CD A:GLU63 3.0 15.6 1.0
CZ A:TYR188 3.1 12.2 1.0
CE1 A:HIS249 3.1 14.1 1.0
CD2 A:HIS249 3.2 14.1 1.0
CG A:GLU63 3.4 15.3 1.0
CE2 A:TYR95 3.6 14.2 1.0
O1 A:CO3600 3.6 10.1 1.0
CE1 A:TYR188 3.8 12.2 1.0
O A:HOH771 3.9 21.8 1.0
CE2 A:TYR188 4.0 12.3 1.0
CE1 A:TYR95 4.0 14.4 1.0
OE1 A:GLU63 4.1 15.4 1.0
ND1 A:HIS249 4.3 13.9 1.0
CG A:HIS249 4.3 14.1 1.0
NH2 A:ARG124 4.4 15.8 1.0
CB A:SER125 4.5 12.6 1.0
N A:ALA126 4.7 12.6 1.0
CB A:GLU63 4.7 15.3 1.0
NZ A:LYS296 4.8 11.9 1.0
NE A:ARG124 4.8 15.4 1.0
N A:SER125 4.8 13.1 1.0
CD2 A:TYR95 4.9 14.4 1.0
OG A:SER125 5.0 12.5 1.0

Reference:

H.M.Baker, Q.-Y.He, S.K.Briggs, A.B.Mason, E.N.Baker. Structural and Functional Consequences of Binding Site Mutations in Transferrin: Crystal Structures of the ASP63GLU and ARG124ALA Mutants of the N-Lobe of Human Transferrin Biochemistry V. 42 7084 2003.
ISSN: ISSN 0006-2960
PubMed: 12795604
DOI: 10.1021/BI020689F
Page generated: Sat Aug 3 12:34:38 2024

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