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Iron in PDB 1n7w: Crystal Structure of Human Serum Transferrin, N-Lobe L66W Mutant

Protein crystallography data

The structure of Crystal Structure of Human Serum Transferrin, N-Lobe L66W Mutant, PDB code: 1n7w was solved by T.E.Adams, A.B.Mason, Q.Y.He, P.J.Halbrooks, S.K.Briggs, V.C.Smith, R.T.Macgillivray, S.J.Everse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.46 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.183, 57.916, 135.513, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 23.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Serum Transferrin, N-Lobe L66W Mutant (pdb code 1n7w). 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 Human Serum Transferrin, N-Lobe L66W Mutant, PDB code: 1n7w:

Iron binding site 1 out of 1 in 1n7w

Go back to Iron Binding Sites List in 1n7w
Iron binding site 1 out of 1 in the Crystal Structure of Human Serum Transferrin, N-Lobe L66W Mutant


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 Human Serum Transferrin, N-Lobe L66W Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe339

b:19.8
occ:1.00
OH A:TYR188 2.0 20.1 1.0
OH A:TYR95 2.1 16.0 1.0
OD1 A:ASP63 2.2 19.0 1.0
NE2 A:HIS249 2.2 11.5 1.0
O1 A:CO3338 2.4 18.6 1.0
O2 A:CO3338 2.4 18.6 1.0
C A:CO3338 2.8 18.8 1.0
CD2 A:HIS249 3.1 11.9 1.0
CZ A:TYR95 3.1 15.9 1.0
CZ A:TYR188 3.1 18.7 1.0
CG A:ASP63 3.2 16.9 1.0
CE1 A:HIS249 3.2 11.6 1.0
CB A:ASP63 3.7 15.7 1.0
CE2 A:TYR95 3.7 13.5 1.0
O A:HOH414 3.8 16.4 1.0
CE2 A:TYR188 3.9 18.5 1.0
CE1 A:TYR188 4.0 18.6 1.0
O3 A:CO3338 4.0 18.7 1.0
CE1 A:TYR95 4.1 15.0 1.0
OD2 A:ASP63 4.2 17.9 1.0
CG A:HIS249 4.3 12.8 1.0
ND1 A:HIS249 4.3 13.6 1.0
NH2 A:ARG124 4.3 21.1 1.0
CA A:ASP63 4.4 14.8 1.0
NZ A:LYS296 4.4 15.8 1.0
CB A:SER125 4.6 18.3 1.0
NE A:ARG124 4.8 20.3 1.0
CD A:LYS296 4.9 12.8 1.0
N A:ALA126 4.9 18.1 1.0
OG A:SER125 5.0 16.8 1.0
N A:SER125 5.0 18.1 1.0

Reference:

T.E.Adams, A.B.Mason, Q.Y.He, P.J.Halbrooks, S.K.Briggs, V.C.Smith, R.T.Macgillivray, S.J.Everse. The Position of Arginine 124 Controls the Rate of Iron Release From the N-Lobe of Human Serum Transferrin. A Structural Study J.Biol.Chem. V. 278 6027 2003.
ISSN: ISSN 0021-9258
PubMed: 12458193
DOI: 10.1074/JBC.M210349200
Page generated: Sun Dec 13 14:25:13 2020

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