Iron in PDB 7d3f: Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State

All present enzymatic activity of Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State:
1.6.3.1;

The structure of Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State also contains other interesting chemical elements:

Calcium	(Ca)	4 atoms
Sodium	(Na)	4 atoms

The binding sites of Iron atom in the Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State (pdb code 7d3f). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State, PDB code: 7d3f:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1601 b:78.7 occ:1.00 FE A:HEM1601 0.0 78.7 1.0 NE2 A:HIS1130 2.0 54.4 1.0 NE2 A:HIS1225 2.0 57.5 1.0 NB A:HEM1601 2.0 47.6 1.0 ND A:HEM1601 2.0 52.7 1.0 NA A:HEM1601 2.0 53.3 1.0 NC A:HEM1601 2.1 53.6 1.0 CE1 A:HIS1225 2.7 55.8 1.0 CE1 A:HIS1130 2.9 49.9 1.0 CD2 A:HIS1130 3.0 53.3 1.0 C4B A:HEM1601 3.1 46.1 1.0 C1D A:HEM1601 3.1 52.3 1.0 C1B A:HEM1601 3.1 45.0 1.0 C4D A:HEM1601 3.1 52.8 1.0 C1C A:HEM1601 3.1 51.0 1.0 C4A A:HEM1601 3.1 50.0 1.0 C4C A:HEM1601 3.1 51.2 1.0 C1A A:HEM1601 3.1 50.8 1.0 CD2 A:HIS1225 3.2 58.2 1.0 CHD A:HEM1601 3.4 53.5 1.0 CHC A:HEM1601 3.4 45.2 1.0 CHB A:HEM1601 3.4 45.2 1.0 CHA A:HEM1601 3.4 52.3 1.0 ND1 A:HIS1225 4.0 54.4 1.0 ND1 A:HIS1130 4.0 49.1 1.0 CG A:HIS1130 4.1 51.4 1.0 CG A:HIS1225 4.2 57.4 1.0 C3B A:HEM1601 4.3 46.7 1.0 C2D A:HEM1601 4.3 54.8 1.0 C2B A:HEM1601 4.3 44.1 1.0 C3D A:HEM1601 4.3 56.6 1.0 C3A A:HEM1601 4.3 50.6 1.0 C2A A:HEM1601 4.3 50.7 1.0 C2C A:HEM1601 4.3 53.8 1.0 C3C A:HEM1601 4.3 50.2 1.0 CE A:MET1104 4.9 62.5 1.0

Iron binding site 2 out of 4 in the Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1602 b:72.6 occ:1.00 FE A:HEM1602 0.0 72.6 1.0 NE2 A:HIS1238 2.0 50.4 1.0 NE2 A:HIS1144 2.0 45.7 1.0 NA A:HEM1602 2.0 45.3 1.0 NC A:HEM1602 2.0 43.4 1.0 NB A:HEM1602 2.1 46.4 1.0 ND A:HEM1602 2.1 48.5 1.0 CD2 A:HIS1238 2.9 47.8 1.0 CD2 A:HIS1144 2.9 42.7 1.0 CE1 A:HIS1144 3.0 36.9 1.0 CE1 A:HIS1238 3.0 48.3 1.0 C4C A:HEM1602 3.0 43.6 1.0 C1D A:HEM1602 3.1 42.4 1.0 C4A A:HEM1602 3.1 44.2 1.0 C1C A:HEM1602 3.1 39.8 1.0 C1A A:HEM1602 3.1 40.9 1.0 C1B A:HEM1602 3.1 44.1 1.0 C4D A:HEM1602 3.1 45.2 1.0 C4B A:HEM1602 3.1 44.6 1.0 CHD A:HEM1602 3.4 44.7 1.0 CHB A:HEM1602 3.4 46.7 1.0 CHC A:HEM1602 3.4 43.9 1.0 CHA A:HEM1602 3.4 43.3 1.0 ND1 A:HIS1144 4.0 40.3 1.0 ND1 A:HIS1238 4.0 48.5 1.0 CG A:HIS1144 4.0 42.1 1.0 CG A:HIS1238 4.1 46.7 1.0 C3C A:HEM1602 4.3 40.8 1.0 C2C A:HEM1602 4.3 42.7 1.0 C3A A:HEM1602 4.3 43.0 1.0 C2D A:HEM1602 4.3 43.3 1.0 C2A A:HEM1602 4.3 45.7 1.0 C3D A:HEM1602 4.3 45.8 1.0 C2B A:HEM1602 4.3 45.9 1.0 C3B A:HEM1602 4.3 44.0 1.0 NE2 A:HIS1148 4.4 56.2 1.0 CD2 A:HIS1148 4.4 50.8 1.0

Iron binding site 3 out of 4 in the Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1601 b:77.3 occ:1.00 FE C:HEM1601 0.0 77.3 1.0 ND C:HEM1601 2.0 56.7 1.0 NC C:HEM1601 2.0 56.8 1.0 NA C:HEM1601 2.0 56.5 1.0 NB C:HEM1601 2.1 50.7 1.0 NE2 C:HIS1225 2.5 54.8 1.0 NE2 C:HIS1130 2.5 56.3 1.0 C1D C:HEM1601 3.0 55.2 1.0 C4D C:HEM1601 3.1 56.0 1.0 C4C C:HEM1601 3.1 54.0 1.0 C4B C:HEM1601 3.1 48.0 1.0 C1A C:HEM1601 3.1 53.2 1.0 C4A C:HEM1601 3.1 52.6 1.0 C1C C:HEM1601 3.1 53.4 1.0 C1B C:HEM1601 3.1 47.2 1.0 CD2 C:HIS1130 3.2 54.8 1.0 CE1 C:HIS1225 3.4 58.7 1.0 CHD C:HEM1601 3.4 56.1 1.0 CHA C:HEM1601 3.4 54.8 1.0 CHB C:HEM1601 3.4 47.5 1.0 CHC C:HEM1601 3.4 46.9 1.0 CE1 C:HIS1130 3.5 56.3 1.0 CD2 C:HIS1225 3.5 58.1 1.0 C2D C:HEM1601 4.3 56.5 1.0 C3D C:HEM1601 4.3 58.7 1.0 C2A C:HEM1601 4.3 53.5 1.0 CG C:HIS1130 4.3 56.3 1.0 C3A C:HEM1601 4.3 53.6 1.0 C3B C:HEM1601 4.3 48.4 1.0 C2C C:HEM1601 4.3 55.7 1.0 C2B C:HEM1601 4.3 46.0 1.0 C3C C:HEM1601 4.3 52.1 1.0 ND1 C:HIS1130 4.4 60.0 1.0 ND1 C:HIS1225 4.6 60.9 1.0 CG C:HIS1225 4.6 61.7 1.0 CE C:MET1104 4.8 64.9 1.0

Iron binding site 4 out of 4 in the Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1602 b:74.0 occ:1.00 FE C:HEM1602 0.0 74.0 1.0 NC C:HEM1602 2.0 46.1 1.0 ND C:HEM1602 2.1 51.2 1.0 NB C:HEM1602 2.1 49.0 1.0 NA C:HEM1602 2.1 47.2 1.0 NE2 C:HIS1144 2.5 39.6 1.0 NE2 C:HIS1238 2.5 56.1 1.0 C4C C:HEM1602 3.0 45.6 1.0 C1C C:HEM1602 3.0 41.4 1.0 C1D C:HEM1602 3.0 44.6 1.0 C4B C:HEM1602 3.1 46.4 1.0 C1B C:HEM1602 3.1 45.8 1.0 C4D C:HEM1602 3.1 47.4 1.0 C4A C:HEM1602 3.1 45.5 1.0 C1A C:HEM1602 3.1 42.2 1.0 CD2 C:HIS1144 3.1 39.7 1.0 CE1 C:HIS1238 3.2 51.4 1.0 CD2 C:HIS1238 3.4 57.8 1.0 CHD C:HEM1602 3.4 47.1 1.0 CHC C:HEM1602 3.4 45.1 1.0 CHB C:HEM1602 3.4 47.5 1.0 CHA C:HEM1602 3.5 44.9 1.0 CE1 C:HIS1144 3.5 41.7 1.0 ND1 C:HIS1238 4.1 53.6 1.0 C3C C:HEM1602 4.2 42.5 1.0 C2C C:HEM1602 4.2 44.1 1.0 C2D C:HEM1602 4.3 45.1 1.0 CG C:HIS1238 4.3 50.8 1.0 C3D C:HEM1602 4.3 47.5 1.0 C3A C:HEM1602 4.3 44.4 1.0 C2A C:HEM1602 4.3 47.0 1.0 C2B C:HEM1602 4.3 47.4 1.0 C3B C:HEM1602 4.3 44.8 1.0 CG C:HIS1144 4.3 44.0 1.0 ND1 C:HIS1144 4.5 50.2 1.0 NE2 C:HIS1148 4.5 55.1 1.0 CD2 C:HIS1148 4.5 50.7 1.0

L.Chen, J.X.Wu. Cryo-Em Structure of Human DUOX1-DUOXA1 in High-Calcium State To Be Published.