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Iron in PDB 7enu: Crystal Structure of Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A Resolution

Protein crystallography data

The structure of Crystal Structure of Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A Resolution, PDB code: 7enu was solved by J.Singh, A.Maurya, V.Viswanathan, P.K.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) 77.75 / 2.32
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 155.67, 82.027, 112.137, 90, 129.62, 90
R / Rfree (%) 20.3 / 24.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A Resolution (pdb code 7enu). 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 Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A Resolution, PDB code: 7enu:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 7enu

Go back to Iron Binding Sites List in 7enu
Iron binding site 1 out of 2 in the Crystal Structure of Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A 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 Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe701

b:77.3
occ:1.00
OH A:TYR433 2.0 83.0 1.0
OH A:TYR526 2.0 59.9 1.0
OD1 A:ASP395 2.0 74.0 1.0
O2 A:CO3702 2.1 63.5 1.0
O1 A:CO3702 2.1 64.0 1.0
NE2 A:HIS595 2.3 52.2 1.0
C A:CO3702 2.4 71.5 1.0
CZ A:TYR433 3.0 83.3 1.0
CZ A:TYR526 3.1 50.6 1.0
CG A:ASP395 3.2 62.2 1.0
CD2 A:HIS595 3.2 50.5 1.0
CE1 A:HIS595 3.3 55.2 1.0
CE2 A:TYR433 3.5 82.1 1.0
O A:HOH804 3.5 69.1 1.0
O3 A:CO3702 3.7 65.3 1.0
CB A:ASP395 3.8 58.6 1.0
CE1 A:TYR526 3.9 52.5 1.0
CE2 A:TYR526 4.0 54.1 1.0
O A:HOH821 4.0 68.9 1.0
CE1 A:TYR433 4.0 88.1 1.0
OD2 A:ASP395 4.2 63.0 1.0
NH2 A:ARG463 4.4 66.9 1.0
CG A:HIS595 4.4 47.9 1.0
ND1 A:HIS595 4.4 56.3 1.0
CA A:ASP395 4.5 55.7 1.0
CB A:THR464 4.6 79.1 1.0
N A:ALA465 4.7 64.7 1.0
N A:THR464 4.7 67.4 1.0
NE A:ARG463 4.8 60.7 1.0
CD2 A:TYR433 4.8 82.9 1.0
OG1 A:THR464 4.9 71.5 1.0

Iron binding site 2 out of 2 in 7enu

Go back to Iron Binding Sites List in 7enu
Iron binding site 2 out of 2 in the Crystal Structure of Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A 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 Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe701

b:68.2
occ:1.00
O2 B:CO3702 2.0 51.0 1.0
O1 B:CO3702 2.1 49.0 1.0
OH B:TYR433 2.1 53.3 1.0
OH B:TYR526 2.1 58.9 1.0
OD1 B:ASP395 2.1 67.5 1.0
NE2 B:HIS595 2.2 51.5 1.0
C B:CO3702 2.3 50.7 1.0
CZ B:TYR433 3.0 64.5 1.0
CZ B:TYR526 3.0 56.1 1.0
CG B:ASP395 3.1 56.8 1.0
CD2 B:HIS595 3.2 47.6 1.0
CE1 B:HIS595 3.3 47.4 1.0
CE2 B:TYR433 3.6 62.1 1.0
O3 B:CO3702 3.6 53.1 1.0
CB B:ASP395 3.7 55.0 1.0
CE1 B:TYR526 3.8 55.4 1.0
CE2 B:TYR526 3.9 55.7 1.0
O B:HOH816 3.9 57.5 1.0
CE1 B:TYR433 3.9 74.3 1.0
O B:HOH812 4.0 66.2 1.0
OD2 B:ASP395 4.1 65.8 1.0
NH2 B:ARG463 4.3 62.8 1.0
CG B:HIS595 4.4 42.6 1.0
ND1 B:HIS595 4.4 49.4 1.0
CA B:ASP395 4.4 49.6 1.0
CB B:THR464 4.6 59.2 1.0
N B:THR464 4.6 50.6 1.0
NE B:ARG463 4.6 68.2 1.0
N B:ALA465 4.7 60.7 1.0
OG1 B:THR464 4.8 57.3 1.0
CD2 B:TYR433 4.8 72.3 1.0
CZ B:ARG463 4.9 62.8 1.0

Reference:

J.Singh, A.Maurya, V.Viswanathan, P.K.Singh, P.Sharma, S.Sharma, T.P.Singh. Crystal Structure of Iron-Saturated C-Terminal Half of Lactoferrin Produced Proteolytically Using Pepsin at 2.32A Resolution To Be Published.
Page generated: Wed Aug 6 22:17:46 2025

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