Potassium in PDB 9dqp: Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa)

The structure of Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa), PDB code: 9dqp was solved by Y.-C.Zheng, W.-C.Chang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.96 / 1.95
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	97.052, 42.931, 126.758, 90, 107.03, 90
R / Rfree (%)	19.8 / 25.1

The binding sites of Potassium atom in the Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa) (pdb code 9dqp). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa), PDB code: 9dqp:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa) within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:37.7 occ:1.00 CD2 A:HIS31 3.5 32.4 1.0 CD A:ARG111 3.7 39.9 1.0 NH1 A:ARG111 3.7 51.8 1.0 CA A:LEU108 3.8 12.2 1.0 N A:LEU108 3.9 12.8 1.0 CB A:LEU108 4.0 10.3 1.0 CG A:HIS31 4.2 20.1 1.0 CD1 A:LEU28 4.2 25.4 1.0 CD1 A:LEU108 4.2 13.5 1.0 C A:PRO107 4.3 20.4 1.0 CB A:HIS31 4.3 18.1 1.0 O A:HOH411 4.4 39.1 1.0 CG A:PRO107 4.4 23.2 1.0 NE2 A:HIS31 4.5 22.1 1.0 CB A:ARG111 4.5 17.9 1.0 O A:PRO107 4.6 13.4 1.0 CB A:PRO107 4.6 24.4 1.0 NE A:ARG111 4.6 45.3 1.0 CZ A:ARG111 4.6 50.5 1.0 CG A:LEU108 4.7 12.3 1.0 CG A:ARG111 4.7 25.8 1.0 OE2 A:GLU27 5.0 60.9 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Apo-Hrmj From Streptomyces Sp. AG109_G2-6 (Hrmj- Ssa) within 5.0Å range: probe atom residue distance (Å) B Occ B:K303 b:56.9 occ:1.00 N B:ILE215 2.5 23.4 1.0 O B:HOH487 3.0 28.1 1.0 CA B:PRO214 3.1 19.2 1.0 C B:PRO214 3.2 19.4 1.0 CG1 B:ILE215 3.2 21.6 1.0 O B:ILE215 3.4 29.2 1.0 CA B:ILE215 3.5 27.7 1.0 CB B:PRO214 3.6 28.4 1.0 CG2 B:ILE141 3.9 35.4 1.0 CB B:ILE215 3.9 24.9 1.0 C B:ILE215 3.9 38.0 1.0 CG B:ARG53 4.4 56.7 1.0 N B:PRO214 4.4 24.6 1.0 O B:PRO214 4.4 22.6 1.0 CZ B:ARG53 4.4 65.2 1.0 CD1 B:ILE215 4.5 23.5 1.0 CG2 B:ILE215 4.5 24.8 1.0 O B:ARG213 4.5 22.2 1.0 NH2 B:ARG53 4.6 51.8 1.0 NE B:ARG53 4.6 57.3 1.0 OG B:SER143 4.7 35.3 1.0 CB B:SER143 4.7 28.1 1.0 NH1 B:ARG53 4.7 58.0 1.0 CG B:PRO214 4.8 29.5 1.0 C B:ARG213 4.9 25.8 1.0

Y.C.Zheng, X.Li, L.Cha, J.C.Paris, C.Michael, R.Ushimaru, Y.Ogasawara, I.Abe, Y.Guo, W.C.Chang. Comparison of A Nonheme Iron Cyclopropanase with A Homologous Hydroxylase Reveals Mechanistic Features Associated with Distinct Reaction Outcomes. J.Am.Chem.Soc. 2025.
ISSN: ESSN 1520-5126
PubMed: 39901767
DOI: 10.1021/JACS.4C17741