Gold in PDB 9h4v: Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)

The structure of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form), PDB code: 9h4v was solved by R.Troisi, F.Galardo, L.Messori, F.Sica, A.Merlino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	89.25 / 3.02
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	84.472, 99.714, 198.388, 90, 90, 90
R / Rfree (%)	24.3 / 29.7

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 21;

Binding sites:

The binding sites of Gold atom in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) (pdb code 9h4v). This binding sites where shown within 5.0 Angstroms radius around Gold atom.
In total 21 binding sites of Gold where determined in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form), PDB code: 9h4v:
Jump to Gold binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Gold binding site 1 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 1 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au705 b:71.8 occ:0.65 ND1 A:HIS273 2.2 77.6 1.0 CE1 A:HIS273 3.1 77.7 1.0 CG A:HIS273 3.2 78.5 1.0 CB A:HIS273 3.6 79.9 1.0 CG1 A:VAL29 3.6 103.5 1.0 CA A:HIS273 4.0 81.9 1.0 O A:HIS273 4.1 80.7 1.0 NE2 A:HIS273 4.3 78.7 1.0 CD2 A:HIS273 4.3 78.1 1.0 CB A:VAL29 4.4 104.2 1.0 C A:HIS273 4.5 81.4 1.0 CG2 A:VAL29 5.0 104.5 1.0

Gold binding site 2 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 2 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au706 b:103.1 occ:0.70 CD2 A:HIS473 2.7 133.5 1.0 NE2 A:HIS473 2.7 133.8 1.0 CG A:HIS473 3.9 134.1 1.0 CE1 A:HIS473 4.0 135.1 1.0 ND1 A:HIS473 4.6 135.8 1.0 CB A:HIS473 5.0 131.8 1.0

Gold binding site 3 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 3 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au707 b:99.0 occ:0.30 ND1 A:HIS642 2.9 124.2 1.0 CE1 A:HIS642 3.3 125.4 1.0 CG A:HIS642 4.0 122.0 1.0 NE2 A:HIS642 4.5 125.4 1.0 AU A:AU711 4.5 80.8 0.2 CA A:HIS642 4.6 113.9 1.0 CB A:HIS642 4.7 117.7 1.0 CD A:LYS640 4.7 94.3 1.0 CD2 A:HIS642 4.9 123.4 1.0 CE1 A:HIS598 4.9 88.8 1.0

Gold binding site 4 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 4 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au708 b:97.5 occ:0.20 ND1 A:HIS25 2.2 84.6 1.0 OE2 A:GLU281 3.0 96.7 1.0 CG A:HIS25 3.0 84.1 1.0 CE1 A:HIS25 3.2 83.9 1.0 CD A:GLU281 3.2 94.6 1.0 CB A:HIS25 3.3 84.3 1.0 CA A:HIS25 3.6 86.4 1.0 OE1 A:GLU281 3.6 93.5 1.0 OG A:SER28 3.6 94.9 1.0 CG A:GLU281 3.9 93.5 1.0 CE1 A:PHE274 3.9 83.1 1.0 O A:HIS25 3.9 90.7 1.0 CZ A:PHE274 4.0 82.5 1.0 CD2 A:HIS25 4.1 83.9 1.0 NE2 A:HIS25 4.2 84.0 1.0 C A:HIS25 4.2 89.3 1.0 CB A:GLU281 4.7 91.3 1.0 N A:HIS25 4.8 85.1 1.0 CB A:SER28 4.9 96.5 1.0

Gold binding site 5 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 5 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au709 b:95.8 occ:0.20 AU A:AU709 0.0 95.8 0.2 OE2 A:GLU419 2.4 132.6 1.0 ND1 A:HIS606 2.5 93.8 0.5 CD2 A:HIS606 2.8 95.1 0.5 CE1 A:HIS606 2.9 93.6 0.5 CD A:GLU419 3.5 130.0 1.0 AU A:AU709 3.6 77.2 0.2 NE2 A:HIS606 3.6 95.0 0.5 CG A:HIS606 3.8 94.3 0.5 CG A:HIS606 3.9 95.3 0.5 CA A:HIS606 4.1 94.3 1.0 OE1 A:GLU419 4.1 130.3 1.0 O A:GLN605 4.1 96.1 1.0 NE2 A:HIS606 4.2 93.7 0.5 CB A:HIS606 4.5 95.1 0.5 CB A:HIS606 4.5 94.5 0.5 N A:HIS606 4.5 94.4 1.0 C A:GLN605 4.6 94.6 1.0 CD2 A:HIS606 4.6 94.0 0.5 CG A:GLU419 4.6 126.9 1.0 CG A:GLN605 4.7 92.8 1.0 CE1 A:HIS606 4.8 95.2 0.5 ND1 A:HIS606 5.0 95.5 0.5

Gold binding site 6 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 6 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au709 b:95.8 occ:0.20 ND1 A:HIS606 2.2 95.5 0.5 CD2 A:HIS606 2.2 94.0 0.5 CE1 A:HIS606 2.7 95.2 0.5 NE2 A:HIS606 3.0 93.7 0.5 CG A:HIS606 3.3 94.3 0.5 CG A:HIS606 3.3 95.3 0.5 NE2 A:HIS606 3.8 95.0 0.5 CB A:HIS606 3.9 94.5 0.5 CB A:HIS606 3.9 95.1 0.5 CE1 A:HIS606 4.1 93.6 0.5 CD2 A:HIS606 4.1 95.1 0.5 ND1 A:HIS606 4.2 93.8 0.5 CA A:GLN603 4.9 96.9 1.0

Gold binding site 7 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 7 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au709 b:77.2 occ:0.20 AU A:AU709 0.0 77.2 0.2 ND1 A:HIS606 3.2 93.8 0.5 AU A:AU709 3.6 95.8 0.2 CG A:HIS606 3.6 94.3 0.5 CE1 A:HIS606 3.7 93.6 0.5 CD2 A:HIS606 3.8 95.1 0.5 CG A:HIS606 3.9 95.3 0.5 CB A:HIS606 4.0 94.5 0.5 CB A:HIS606 4.0 95.1 0.5 CD2 A:HIS606 4.3 94.0 0.5 NE2 A:HIS606 4.3 93.7 0.5 CA A:HIS606 4.4 94.3 1.0 NE2 A:HIS606 4.6 95.0 0.5 O A:HIS606 4.6 92.9 1.0 ND1 A:HIS606 4.7 95.5 0.5 C A:HIS606 4.9 93.3 1.0

Gold binding site 8 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 8 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au710 b:76.3 occ:0.20 OD1 A:ASP63 2.4 74.7 1.0 NE2 A:HIS249 2.5 61.0 1.0 CE1 A:HIS249 3.4 61.0 1.0 CD2 A:HIS249 3.4 60.5 1.0 CG A:ASP63 3.4 72.5 1.0 NZ A:LYS296 3.7 75.9 1.0 OH A:TYR45 3.7 65.0 1.0 OD2 A:ASP63 3.8 74.3 1.0 CZ A:TYR45 4.4 63.6 1.0 ND1 A:HIS249 4.5 60.5 1.0 CG A:HIS249 4.5 60.1 1.0 N A:ASP63 4.5 64.3 1.0 O A:THR61 4.7 61.5 1.0 CB A:ASP63 4.7 68.5 1.0 CE A:LYS296 4.8 74.5 1.0 CE1 A:TYR45 4.9 63.0 1.0 C A:LEU62 5.0 62.5 1.0

Gold binding site 9 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 9 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au711 b:80.8 occ:0.20 ND1 A:HIS598 2.8 88.5 1.0 CG A:HIS598 3.6 87.8 1.0 CB A:HIS598 3.7 85.5 1.0 CE1 A:HIS598 3.8 88.8 1.0 CA A:ALA595 4.4 81.5 1.0 CD A:LYS640 4.5 94.3 1.0 AU A:AU707 4.5 99.0 0.3 O A:ALA595 4.5 82.1 1.0 O A:GLU594 4.8 79.7 1.0 CD2 A:HIS598 4.8 88.4 1.0 CE A:LYS640 4.8 96.6 1.0 NE2 A:HIS598 4.9 88.7 1.0 NZ A:LYS640 4.9 97.0 1.0 C A:ALA595 5.0 82.1 1.0

Gold binding site 10 out of 21 in the Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form)


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 10 of Crystal Structure of the Adduct Formed Upon Reaction of Aurothiomalate with Human Serum Transferrin (Apo-Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Au712 b:90.5 occ:0.50 ND1 A:HIS207 2.2 77.9 1.0 CE1 A:HIS207 2.9 77.5 1.0 CZ A:TYR238 3.3 83.3 1.0 CG A:HIS207 3.4 75.9 1.0 OH A:TYR238 3.4 83.4 1.0 CE1 A:TYR238 3.5 83.3 1.0 CE2 A:PHE211 3.6 87.2 1.0 CD2 A:PHE211 3.8 85.7 1.0 CE2 A:TYR238 3.9 83.3 1.0 CB A:HIS207 3.9 71.8 1.0 CD1 A:TYR238 4.1 82.9 1.0 NE2 A:HIS207 4.1 76.7 1.0 C A:HIS207 4.2 67.9 1.0 O A:HIS207 4.2 69.1 1.0 CA A:SER208 4.2 66.9 1.0 N A:SER208 4.3 67.5 1.0 CD2 A:HIS207 4.4 76.2 1.0 CB A:SER208 4.4 65.5 1.0 CD2 A:TYR238 4.5 82.7 1.0 CG A:TYR238 4.6 82.1 1.0 CA A:HIS207 4.7 67.8 1.0 CZ A:PHE211 4.9 87.5 1.0

R.Troisi, F.Galardo, L.Messori, F.Sica, A.Merlino. Crystal Structure of the Adduct Formed Upon Reaction of Myochrysine with Human Serum Transferrin (Apo Form) To Be Published.