Zinc in PDB 5od1: Structure of the Engineered Metalloesterase MID1SC10 Complexed with A Phosphonate Transition State Analogue

The structure of Structure of the Engineered Metalloesterase MID1SC10 Complexed with A Phosphonate Transition State Analogue, PDB code: 5od1 was solved by P.R.E.Mittl, S.Studer, D.A.Hansen, D.Hilvert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.00 / 1.34
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	32.349, 46.877, 112.621, 90.00, 90.00, 90.00
R / Rfree (%)	12.6 / 17.1

The binding sites of Zinc atom in the Structure of the Engineered Metalloesterase MID1SC10 Complexed with A Phosphonate Transition State Analogue (pdb code 5od1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of the Engineered Metalloesterase MID1SC10 Complexed with A Phosphonate Transition State Analogue, PDB code: 5od1:

Zinc binding site 1 out of 1 in the Structure of the Engineered Metalloesterase MID1SC10 Complexed with A Phosphonate Transition State Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Engineered Metalloesterase MID1SC10 Complexed with A Phosphonate Transition State Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:14.3 occ:1.00 O1 A:9RQ102 1.8 13.5 1.0 NE2 A:HIS61 2.0 13.7 1.0 ND1 A:HIS35 2.0 14.5 1.0 NE2 A:HIS65 2.0 15.6 1.0 CE1 A:HIS35 2.9 16.3 1.0 CD2 A:HIS61 3.0 15.3 1.0 CE1 A:HIS65 3.0 17.1 1.0 CE1 A:HIS61 3.0 16.0 1.0 HB2 A:HIS35 3.0 13.6 1.0 HE1 A:HIS35 3.1 16.3 1.0 CD2 A:HIS65 3.1 16.2 1.0 CG A:HIS35 3.1 15.1 1.0 HE1 A:HIS65 3.1 16.9 1.0 P1 A:9RQ102 3.2 15.3 1.0 HD2 A:HIS61 3.2 15.0 1.0 HE1 A:HIS61 3.2 15.9 1.0 HD2 A:HIS65 3.3 16.0 1.0 CB A:HIS35 3.5 13.4 1.0 H10 A:9RQ102 3.5 20.5 1.0 HA A:HIS35 3.6 12.7 1.0 O8 A:9RQ102 3.6 17.6 1.0 H5 A:9RQ102 4.0 18.3 1.0 NE2 A:HIS35 4.1 19.0 1.0 CA A:HIS35 4.1 12.3 1.0 C4 A:9RQ102 4.1 17.8 1.0 CG A:HIS61 4.1 16.6 1.0 ND1 A:HIS65 4.1 16.9 1.0 ND1 A:HIS61 4.1 16.1 1.0 CG A:HIS65 4.2 15.3 1.0 CD2 A:HIS35 4.2 19.1 1.0 C3 A:9RQ102 4.3 16.5 1.0 O2 A:9RQ102 4.3 16.8 1.0 C10 A:9RQ102 4.3 21.3 1.0 HB3 A:HIS35 4.4 13.6 1.0 HH12 A:ARG68 4.4 22.7 1.0 C1 A:9RQ102 4.4 17.2 1.0 C5 A:9RQ102 4.7 21.2 1.0 O A:HOH282 4.7 52.1 1.0 C9 A:9RQ102 4.8 17.3 1.0 H1 A:9RQ102 4.8 17.4 1.0 HE2 A:HIS35 4.8 18.4 0.0 H6 A:9RQ102 4.9 19.9 1.0 HD1 A:HIS65 4.9 16.7 0.0 C A:HIS35 4.9 13.3 1.0 HD1 A:HIS61 4.9 15.7 0.0

S.Studer, D.A.Hansen, Z.L.Pianowski, P.R.E.Mittl, A.Debon, S.L.Guffy, B.S.Der, B.Kuhlman, D.Hilvert. Evolution of A Highly Active and Enantiospecific Metalloenzyme From Short Peptides. Science V. 362 1285 2018.
ISSN: ESSN 1095-9203
PubMed: 30545884
DOI: 10.1126/SCIENCE.AAU3744