Iron in PDB 3t0g: Isph:Hmbpp (Substrate) Structure of the T167C Mutant

All present enzymatic activity of Isph:Hmbpp (Substrate) Structure of the T167C Mutant:
1.17.1.2;

The structure of Isph:Hmbpp (Substrate) Structure of the T167C Mutant, PDB code: 3t0g was solved by I.Span, T.Graewert, A.Bacher, W.Eisenreich, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.540, 80.850, 112.560, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 27.8

The binding sites of Iron atom in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant (pdb code 3t0g). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant, PDB code: 3t0g:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Isph:Hmbpp (Substrate) Structure of the T167C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe997 b:21.5 occ:1.00 FE1 A:F3S997 0.0 21.5 1.0 SG A:CYS12 2.2 21.8 1.0 S2 A:F3S997 2.3 20.0 1.0 S3 A:F3S997 2.3 22.9 1.0 S1 A:F3S997 2.4 22.1 1.0 FE3 A:F3S997 2.7 26.3 1.0 FE4 A:F3S997 2.7 21.8 1.0 CB A:CYS12 3.2 16.9 1.0 S4 A:F3S997 3.9 25.8 1.0 N A:GLY14 4.2 15.3 1.0 C28 A:H6P998 4.3 17.9 1.0 N A:VAL15 4.3 14.8 1.0 CG2 A:VAL15 4.4 12.4 1.0 C27 A:H6P998 4.4 14.7 1.0 CA A:GLY14 4.4 15.2 1.0 CB A:ALA268 4.5 17.1 1.0 CB A:ALA199 4.5 21.1 1.0 CA A:CYS12 4.5 18.0 1.0 SG A:CYS96 4.7 20.7 1.0 SG A:CYS197 4.7 21.3 1.0 C A:GLY14 4.8 15.9 1.0 C A:CYS12 4.8 18.3 1.0 C30 A:H6P998 5.0 17.4 1.0 N A:ALA13 5.0 17.4 1.0

Iron binding site 2 out of 6 in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Isph:Hmbpp (Substrate) Structure of the T167C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe997 b:26.3 occ:1.00 FE3 A:F3S997 0.0 26.3 1.0 S3 A:F3S997 2.3 22.9 1.0 S1 A:F3S997 2.3 22.1 1.0 S4 A:F3S997 2.3 25.8 1.0 SG A:CYS197 2.4 21.3 1.0 FE1 A:F3S997 2.7 21.5 1.0 FE4 A:F3S997 2.8 21.8 1.0 CB A:CYS197 3.2 22.4 1.0 S2 A:F3S997 3.8 20.0 1.0 CB A:ALA199 4.2 21.1 1.0 OG1 A:THR200 4.4 18.2 1.0 CD1 A:LEU98 4.6 21.0 1.0 CB A:CYS167 4.7 20.7 1.0 CA A:CYS197 4.7 22.2 1.0 SG A:CYS12 4.8 21.8 1.0 O A:HOH317 4.8 14.8 1.0 SG A:CYS96 4.8 20.7 1.0 CG2 A:THR168 4.9 25.2 1.0 C27 A:H6P998 4.9 14.7 1.0 N A:ALA199 5.0 19.8 1.0

Iron binding site 3 out of 6 in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Isph:Hmbpp (Substrate) Structure of the T167C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe997 b:21.8 occ:1.00 FE4 A:F3S997 0.0 21.8 1.0 S2 A:F3S997 2.2 20.0 1.0 SG A:CYS96 2.2 20.7 1.0 S4 A:F3S997 2.3 25.8 1.0 S3 A:F3S997 2.3 22.9 1.0 FE1 A:F3S997 2.7 21.5 1.0 FE3 A:F3S997 2.8 26.3 1.0 CB A:CYS96 3.0 15.7 1.0 CA A:GLY14 4.1 15.2 1.0 S1 A:F3S997 4.1 22.1 1.0 N A:GLY14 4.4 15.3 1.0 CB A:LEU98 4.4 21.3 1.0 CA A:CYS96 4.5 16.7 1.0 CD1 A:LEU98 4.5 21.0 1.0 SG A:CYS12 4.6 21.8 1.0 C30 A:H6P998 4.8 17.4 1.0 CG A:LEU98 4.8 20.8 1.0 C A:GLY14 4.9 15.9 1.0 C27 A:H6P998 4.9 14.7 1.0 C31 A:H6P998 4.9 18.7 1.0 SG A:CYS197 5.0 21.3 1.0

Iron binding site 4 out of 6 in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Isph:Hmbpp (Substrate) Structure of the T167C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe997 b:20.2 occ:1.00 FE1 B:F3S997 0.0 20.2 1.0 SG B:CYS12 2.1 15.3 1.0 S2 B:F3S997 2.3 19.8 1.0 S1 B:F3S997 2.3 25.7 1.0 S3 B:F3S997 2.3 17.8 1.0 FE3 B:F3S997 2.6 23.1 1.0 FE4 B:F3S997 2.7 21.9 1.0 CB B:CYS12 3.2 14.8 1.0 S4 B:F3S997 3.9 22.3 1.0 N B:VAL15 4.3 16.0 1.0 C28 B:H6P998 4.3 12.5 1.0 CB B:ALA268 4.3 14.3 1.0 N B:GLY14 4.3 16.0 1.0 CG2 B:VAL15 4.4 10.2 1.0 C27 B:H6P998 4.4 13.9 1.0 CA B:GLY14 4.4 16.7 1.0 CA B:CYS12 4.5 15.9 1.0 CB B:ALA199 4.6 18.3 1.0 SG B:CYS197 4.7 20.2 1.0 SG B:CYS96 4.7 22.1 1.0 C B:GLY14 4.8 15.9 1.0 C30 B:H6P998 4.8 16.7 1.0 C B:CYS12 4.8 16.3 1.0

Iron binding site 5 out of 6 in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Isph:Hmbpp (Substrate) Structure of the T167C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe997 b:23.1 occ:1.00 FE3 B:F3S997 0.0 23.1 1.0 S1 B:F3S997 2.3 25.7 1.0 S4 B:F3S997 2.3 22.3 1.0 S3 B:F3S997 2.3 17.8 1.0 SG B:CYS197 2.4 20.2 1.0 FE1 B:F3S997 2.6 20.2 1.0 FE4 B:F3S997 2.8 21.9 1.0 CB B:CYS197 3.3 20.6 1.0 S2 B:F3S997 3.7 19.8 1.0 CB B:ALA199 4.5 18.3 1.0 OG1 B:THR200 4.5 18.7 1.0 SG B:CYS12 4.6 15.3 1.0 CB B:CYS167 4.7 20.6 1.0 CG2 B:THR168 4.7 23.2 1.0 CA B:CYS197 4.7 21.2 1.0 CD1 B:LEU98 4.8 17.2 1.0 C27 B:H6P998 4.8 13.9 1.0 SG B:CYS96 4.8 22.1 1.0 CB B:CYS12 5.0 14.8 1.0

Iron binding site 6 out of 6 in the Isph:Hmbpp (Substrate) Structure of the T167C Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Isph:Hmbpp (Substrate) Structure of the T167C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe997 b:21.9 occ:1.00 FE4 B:F3S997 0.0 21.9 1.0 SG B:CYS96 2.2 22.1 1.0 S4 B:F3S997 2.3 22.3 1.0 S2 B:F3S997 2.3 19.8 1.0 S3 B:F3S997 2.3 17.8 1.0 FE1 B:F3S997 2.7 20.2 1.0 FE3 B:F3S997 2.8 23.1 1.0 CB B:CYS96 3.0 20.7 1.0 S1 B:F3S997 4.0 25.7 1.0 CA B:GLY14 4.1 16.7 1.0 CB B:LEU98 4.4 19.9 1.0 CD1 B:LEU98 4.5 17.2 1.0 CA B:CYS96 4.5 19.1 1.0 SG B:CYS12 4.5 15.3 1.0 N B:GLY14 4.5 16.0 1.0 C30 B:H6P998 4.7 16.7 1.0 C31 B:H6P998 4.8 16.6 1.0 C21 B:H6P998 4.8 15.3 1.0 CG B:LEU98 4.9 19.1 1.0 C B:GLY14 4.9 15.9 1.0 SG B:CYS197 4.9 20.2 1.0 C27 B:H6P998 5.0 13.9 1.0

I.Span, T.Grawert, A.Bacher, W.Eisenreich, M.Groll. Crystal Structures of Mutant Isph Proteins Reveal A Rotation of the Substrate'S Hydroxymethyl Group During Catalysis. J.Mol.Biol. V. 416 1 2012.
ISSN: ISSN 0022-2836
PubMed: 22137895
DOI: 10.1016/J.JMB.2011.11.033