Iron in PDB 3szu: Isph:Hmbpp Complex Structure of E126Q Mutant

All present enzymatic activity of Isph:Hmbpp Complex Structure of E126Q Mutant:
1.17.1.2;

The structure of Isph:Hmbpp Complex Structure of E126Q Mutant, PDB code: 3szu 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 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.190, 80.390, 112.010, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.5

The binding sites of Iron atom in the Isph:Hmbpp Complex Structure of E126Q Mutant (pdb code 3szu). 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 Complex Structure of E126Q Mutant, PDB code: 3szu:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in the Isph:Hmbpp Complex Structure of E126Q 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 Complex Structure of E126Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe997 b:5.3 occ:1.00 FE1 A:F3S997 0.0 5.3 1.0 S2 A:F3S997 2.2 5.4 1.0 S1 A:F3S997 2.3 5.9 1.0 S3 A:F3S997 2.3 5.2 1.0 SG A:CYS12 2.3 5.6 1.0 FE3 A:F3S997 2.6 5.5 1.0 FE4 A:F3S997 2.7 5.1 1.0 CB A:CYS12 3.3 5.8 1.0 S4 A:F3S997 3.9 6.6 1.0 C28 A:H6P998 4.1 6.2 1.0 N A:GLY14 4.2 5.0 1.0 C27 A:H6P998 4.2 6.5 1.0 CA A:GLY14 4.3 6.4 1.0 N A:VAL15 4.4 6.4 1.0 CB A:ALA268 4.4 6.7 1.0 CG2 A:VAL15 4.5 6.9 1.0 CB A:ALA199 4.5 6.0 1.0 CA A:CYS12 4.6 4.9 1.0 SG A:CYS197 4.7 6.5 1.0 SG A:CYS96 4.7 5.2 1.0 C A:GLY14 4.8 6.7 1.0 C30 A:H6P998 4.8 5.7 1.0 C A:CYS12 4.9 6.9 1.0 N A:ALA13 4.9 7.2 1.0

Iron binding site 2 out of 6 in the Isph:Hmbpp Complex Structure of E126Q 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 Complex Structure of E126Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe997 b:5.5 occ:1.00 FE3 A:F3S997 0.0 5.5 1.0 S1 A:F3S997 2.2 5.9 1.0 S4 A:F3S997 2.3 6.6 1.0 SG A:CYS197 2.3 6.5 1.0 S3 A:F3S997 2.4 5.2 1.0 FE1 A:F3S997 2.6 5.3 1.0 FE4 A:F3S997 2.7 5.1 1.0 CB A:CYS197 3.3 5.9 1.0 S2 A:F3S997 3.8 5.4 1.0 CB A:ALA199 4.3 6.0 1.0 OG1 A:THR167 4.4 6.4 1.0 OG1 A:THR200 4.5 6.3 1.0 CA A:CYS197 4.7 6.0 1.0 CG2 A:THR168 4.7 5.6 1.0 CB A:THR167 4.7 4.7 1.0 SG A:CYS12 4.7 5.6 1.0 O A:HOH349 4.8 6.7 1.0 CD1 A:LEU98 4.8 8.0 1.0 C27 A:H6P998 4.8 6.5 1.0 SG A:CYS96 4.8 5.2 1.0

Iron binding site 3 out of 6 in the Isph:Hmbpp Complex Structure of E126Q 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 Complex Structure of E126Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe997 b:5.1 occ:1.00 FE4 A:F3S997 0.0 5.1 1.0 S2 A:F3S997 2.2 5.4 1.0 S4 A:F3S997 2.3 6.6 1.0 S3 A:F3S997 2.3 5.2 1.0 SG A:CYS96 2.3 5.2 1.0 FE1 A:F3S997 2.7 5.3 1.0 FE3 A:F3S997 2.7 5.5 1.0 CB A:CYS96 3.1 6.0 1.0 S1 A:F3S997 3.9 5.9 1.0 CA A:GLY14 4.1 6.4 1.0 CB A:LEU98 4.5 5.7 1.0 N A:GLY14 4.5 5.0 1.0 CA A:CYS96 4.6 6.4 1.0 CD1 A:LEU98 4.6 8.0 1.0 SG A:CYS12 4.6 5.6 1.0 CG A:LEU98 4.8 7.7 1.0 SG A:CYS197 4.8 6.5 1.0 C30 A:H6P998 4.8 5.7 1.0 C31 A:H6P998 4.9 7.5 1.0 C27 A:H6P998 4.9 6.5 1.0

Iron binding site 4 out of 6 in the Isph:Hmbpp Complex Structure of E126Q 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 Complex Structure of E126Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe997 b:5.2 occ:1.00 FE1 B:F3S997 0.0 5.2 1.0 S1 B:F3S997 2.2 6.3 1.0 S2 B:F3S997 2.2 5.2 1.0 S3 B:F3S997 2.3 5.2 1.0 SG B:CYS12 2.3 5.8 1.0 FE3 B:F3S997 2.6 5.2 1.0 FE4 B:F3S997 2.7 4.5 1.0 CB B:CYS12 3.2 6.1 1.0 S4 B:F3S997 3.9 4.9 1.0 C28 B:H6P998 4.1 8.6 1.0 N B:GLY14 4.2 6.4 1.0 C27 B:H6P998 4.2 8.5 1.0 CA B:GLY14 4.3 7.1 1.0 CG2 B:VAL15 4.4 7.9 1.0 N B:VAL15 4.4 5.3 1.0 CB B:ALA268 4.4 6.5 1.0 CB B:ALA199 4.5 6.5 1.0 SG B:CYS197 4.7 6.6 1.0 CA B:CYS12 4.7 5.0 1.0 SG B:CYS96 4.7 5.2 1.0 C30 B:H6P998 4.8 6.7 1.0 C B:GLY14 4.8 5.4 1.0 C B:CYS12 4.9 5.4 1.0 N B:ALA13 5.0 5.9 1.0

Iron binding site 5 out of 6 in the Isph:Hmbpp Complex Structure of E126Q 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 Complex Structure of E126Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe997 b:5.2 occ:1.00 FE3 B:F3S997 0.0 5.2 1.0 S1 B:F3S997 2.2 6.3 1.0 S4 B:F3S997 2.3 4.9 1.0 SG B:CYS197 2.3 6.6 1.0 S3 B:F3S997 2.4 5.2 1.0 FE1 B:F3S997 2.6 5.2 1.0 FE4 B:F3S997 2.7 4.5 1.0 CB B:CYS197 3.3 7.8 1.0 S2 B:F3S997 3.8 5.2 1.0 OG1 B:THR167 4.3 5.5 1.0 CB B:ALA199 4.3 6.5 1.0 OG1 B:THR200 4.5 6.8 1.0 CB B:THR167 4.6 5.1 1.0 CG2 B:THR168 4.7 6.2 1.0 CA B:CYS197 4.7 5.4 1.0 O B:HOH327 4.7 8.3 1.0 SG B:CYS12 4.7 5.8 1.0 C27 B:H6P998 4.8 8.5 1.0 SG B:CYS96 4.8 5.2 1.0 CD1 B:LEU98 4.9 7.7 1.0

Iron binding site 6 out of 6 in the Isph:Hmbpp Complex Structure of E126Q 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 Complex Structure of E126Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe997 b:4.5 occ:1.00 FE4 B:F3S997 0.0 4.5 1.0 S2 B:F3S997 2.2 5.2 1.0 S4 B:F3S997 2.2 4.9 1.0 SG B:CYS96 2.3 5.2 1.0 S3 B:F3S997 2.3 5.2 1.0 FE1 B:F3S997 2.7 5.2 1.0 FE3 B:F3S997 2.7 5.2 1.0 CB B:CYS96 3.2 4.6 1.0 S1 B:F3S997 3.9 6.3 1.0 CA B:GLY14 4.2 7.1 1.0 CB B:LEU98 4.4 6.8 1.0 N B:GLY14 4.5 6.4 1.0 CA B:CYS96 4.6 5.6 1.0 SG B:CYS12 4.6 5.8 1.0 CD1 B:LEU98 4.7 7.7 1.0 SG B:CYS197 4.8 6.6 1.0 C30 B:H6P998 4.8 6.7 1.0 CG B:LEU98 4.9 6.4 1.0 C31 B:H6P998 4.9 8.4 1.0 C27 B:H6P998 4.9 8.5 1.0 N B:LEU98 5.0 4.9 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