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Iron in PDB 7evq: Crystal Structure of C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution

Protein crystallography data

The structure of Crystal Structure of C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution, PDB code: 7evq was solved by V.Viswanathan, J.Singh, P.Sharma, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.12 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 153.246, 81.69, 110.227, 90, 129.91, 90
R / Rfree (%) 22.7 / 28.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution (pdb code 7evq). 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 C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution, PDB code: 7evq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 7evq

Go back to Iron Binding Sites List in 7evq
Iron binding site 1 out of 2 in the Crystal Structure of C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution


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 C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe701

b:28.6
occ:1.00
OH A:TYR526 2.0 17.1 1.0
OD2 A:ASP395 2.1 28.9 1.0
NE2 A:HIS595 2.1 16.2 1.0
O1 A:BCT702 2.2 9.7 1.0
O2 A:BCT702 2.2 26.8 1.0
C A:BCT702 2.4 19.8 1.0
OH A:TYR433 2.4 33.6 1.0
CG A:ASP395 2.9 21.3 1.0
CZ A:TYR526 2.9 15.1 1.0
CD2 A:HIS595 3.0 15.6 1.0
CE1 A:HIS595 3.1 12.9 1.0
CZ A:TYR433 3.4 29.2 1.0
CE2 A:TYR526 3.5 19.6 1.0
CB A:ASP395 3.6 18.3 1.0
OD1 A:ASP395 3.7 19.5 1.0
O3 A:BCT702 3.8 12.9 1.0
CE1 A:TYR526 3.9 12.6 1.0
O A:HOH803 4.1 25.0 1.0
CE1 A:TYR433 4.2 39.3 1.0
CG A:HIS595 4.2 12.5 1.0
CE2 A:TYR433 4.2 33.2 1.0
ND1 A:HIS595 4.2 12.5 1.0
CA A:ASP395 4.4 11.9 1.0
NH2 A:ARG463 4.6 12.5 1.0
CZ A:ARG463 4.7 18.9 1.0
CD2 A:TYR526 4.8 26.6 1.0
CB A:THR464 4.9 22.8 1.0
N A:THR464 4.9 28.1 1.0
N A:ALA465 5.0 23.2 1.0
NH1 A:ARG463 5.0 42.4 1.0

Iron binding site 2 out of 2 in 7evq

Go back to Iron Binding Sites List in 7evq
Iron binding site 2 out of 2 in the Crystal Structure of C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution


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 C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe702

b:51.2
occ:1.00
OH B:TYR526 1.7 42.6 1.0
OH B:TYR433 2.0 30.8 1.0
O3 B:BCT703 2.1 33.0 1.0
O2 B:BCT703 2.1 35.4 1.0
OD1 B:ASP395 2.2 41.4 1.0
C B:BCT703 2.3 43.2 1.0
NE2 B:HIS595 2.3 50.9 1.0
CZ B:TYR526 2.9 52.0 1.0
CZ B:TYR433 3.1 56.2 1.0
CD2 B:HIS595 3.2 47.8 1.0
CG B:ASP395 3.2 29.7 1.0
CE1 B:HIS595 3.4 48.0 1.0
CE1 B:TYR526 3.4 51.5 1.0
O1 B:BCT703 3.7 33.1 1.0
CE2 B:TYR433 3.7 52.3 1.0
CB B:ASP395 3.8 25.2 1.0
CE2 B:TYR526 3.9 57.0 1.0
CE1 B:TYR433 4.0 54.2 1.0
OD2 B:ASP395 4.1 31.6 1.0
NH1 B:ARG463 4.1 50.3 1.0
CG B:HIS595 4.4 44.6 1.0
ND1 B:HIS595 4.4 46.0 1.0
CB B:THR464 4.6 26.3 1.0
CA B:ASP395 4.6 20.9 1.0
N B:ALA465 4.6 50.4 1.0
NE B:ARG463 4.6 47.0 1.0
N B:THR464 4.7 29.2 1.0
CD1 B:TYR526 4.8 49.6 1.0
CZ B:ARG463 4.8 37.3 1.0
CB B:ALA465 5.0 51.5 1.0
N B:GLY396 5.0 30.0 1.0
CD2 B:TYR433 5.0 60.4 1.0

Reference:

V.Viswanathan, J.Singh, P.Sharma, S.Sharma, T.P.Singh. Crystal Structure of C-Terminal Half of Lactoferrin Obtained By Limited Proteolysis Using Pepsin at 2.6 A Resolution To Be Published.
Page generated: Wed Aug 6 22:20:32 2025

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