Iron in PDB 5ao4: Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp

The structure of Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp, PDB code: 5ao4 was solved by L.H.Arnold, D.Schwefel, I.A.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.05 / 3.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	197.545, 80.817, 147.665, 90.00, 114.93, 90.00
R / Rfree (%)	24.4 / 30.8

The binding sites of Iron atom in the Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp (pdb code 5ao4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp, PDB code: 5ao4:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp


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 in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1584 b:35.6 occ:1.00 OD1 A:ASP311 2.4 61.6 1.0 OD2 A:ASP207 2.5 56.4 1.0 NE2 A:HIS167 2.6 55.6 1.0 OD2 A:ASP311 2.7 61.9 1.0 CG A:ASP311 2.9 62.1 1.0 CG A:ASP207 3.2 56.3 1.0 OD1 A:ASP207 3.2 56.4 1.0 CD2 A:HIS167 3.4 55.2 1.0 NH1 A:ARG164 3.5 55.2 1.0 CE1 A:HIS167 3.5 55.4 1.0 CB A:ASP311 4.4 63.0 1.0 CG A:HIS167 4.6 54.9 1.0 ND1 A:HIS167 4.6 55.0 1.0 CB A:ASP207 4.6 56.3 1.0 CG2 A:VAL171 4.7 56.7 1.0 CZ A:ARG164 4.8 55.0 1.0 CD2 A:TYR315 4.8 61.1 1.0

Iron binding site 2 out of 4 in the Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp


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 in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1582 b:45.5 occ:1.00 OD1 B:ASP311 2.3 56.1 1.0 OD2 B:ASP207 2.4 55.1 1.0 NE2 B:HIS167 2.5 48.8 1.0 OD2 B:ASP311 2.7 57.4 1.0 CG B:ASP311 2.8 56.7 1.0 OD1 B:ASP207 3.0 56.3 1.0 CG B:ASP207 3.1 55.8 1.0 CD2 B:HIS167 3.2 49.1 1.0 CE1 B:HIS167 3.5 48.2 1.0 NH1 B:ARG164 3.8 50.0 1.0 CB B:ASP311 4.3 56.7 1.0 CG B:HIS167 4.4 48.6 1.0 CG2 B:VAL171 4.5 49.6 1.0 ND1 B:HIS167 4.5 48.0 1.0 CB B:ASP207 4.5 56.0 1.0 CD2 B:TYR315 4.7 57.6 1.0 O B:ASP311 5.0 56.2 1.0

Iron binding site 3 out of 4 in the Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1581 b:54.2 occ:1.00 OD1 C:ASP311 2.6 78.1 1.0 OD2 C:ASP207 2.8 50.5 1.0 OD1 C:ASP207 2.8 49.1 1.0 NE2 C:HIS167 2.8 64.3 1.0 CG C:ASP207 3.1 49.9 1.0 NH1 C:ARG164 3.3 64.6 1.0 OD2 C:ASP311 3.3 80.2 1.0 CG C:ASP311 3.4 79.4 1.0 CE1 C:HIS167 3.6 64.7 1.0 CD2 C:HIS167 3.7 63.8 1.0 CZ C:ARG164 4.6 64.9 1.0 CB C:ASP207 4.7 50.3 1.0 ND1 C:HIS167 4.7 64.5 1.0 CG C:HIS167 4.7 63.9 1.0 CD2 C:TYR315 4.8 77.2 1.0 CB C:ASP311 4.8 79.9 1.0

Iron binding site 4 out of 4 in the Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of in Vitro Phosphorylated Human SAMHD1 (Amino Acid Residues 115-626) Bound to Gtp within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1582 b:76.3 occ:1.00 OD1 D:ASP311 2.3 82.8 1.0 NE2 D:HIS167 2.4 66.9 1.0 OD2 D:ASP207 2.5 0.9 1.0 OD2 D:ASP311 3.0 81.9 1.0 CG D:ASP311 3.0 82.5 1.0 OD1 D:ASP207 3.0 0.5 1.0 CG D:ASP207 3.1 0.3 1.0 CE1 D:HIS167 3.3 66.0 1.0 CD2 D:HIS167 3.4 68.0 1.0 NH1 D:ARG164 4.0 64.1 1.0 CD2 D:TYR315 4.4 79.7 1.0 ND1 D:HIS167 4.4 66.5 1.0 CG D:HIS167 4.5 67.7 1.0 CB D:ASP311 4.5 83.0 1.0 CG2 D:VAL171 4.6 69.7 1.0 CB D:ASP207 4.6 0.5 1.0 CE2 D:TYR315 4.8 79.6 1.0 O D:ASP311 5.0 81.2 1.0

L.H.Arnold, H.C.T.Groom, S.Kunzelmann, D.Schwefel, S.J.Caswell, P.Ordonez, M.C.Mann, S.Rueschenbaum, D.C.Goldstone, S.Pennell, S.A.Howell, J.P.Stoye, M.Webb, I.A.Taylor, K.N.Bishop. Phospho-Dependent Regulation of SAMHD1 Oligomerisation Couples Catalysis and Restriction. Plos Pathog. V. 11 5194 2015.
ISSN: ISSN 1553-7366
PubMed: 26431200
DOI: 10.1371/JOURNAL.PPAT.1005194