Potassium in PDB 6l32: Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution

The structure of Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution, PDB code: 6l32 was solved by P.K.Singh, C.Rani, P.Sharma, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.11 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	79.700, 84.710, 98.750, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 24.4

The structure of Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution also contains other interesting chemical elements:

Zinc	(Zn)	1 atom
Iron	(Fe)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Potassium atom in the Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution (pdb code 6l32). 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 Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution, PDB code: 6l32:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution


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 Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:K609 b:16.9 occ:1.00 O A:HOH817 2.1 20.4 1.0 NE2 A:HIS109 2.1 15.4 1.0 O1D A:HEM608 2.4 20.6 0.7 O A:HOH995 2.7 14.7 1.0 O A:HOH703 3.0 16.4 0.3 CE1 A:HIS109 3.0 16.3 1.0 CD2 A:HIS109 3.1 16.1 1.0 CGD A:HEM608 3.3 19.5 0.7 NA A:HEM608 3.4 16.3 0.3 NA A:HEM608 3.4 16.4 0.7 O2D A:HEM608 3.4 18.3 0.7 ND A:HEM608 3.5 16.6 1.0 C1A A:HEM608 3.5 16.6 0.3 C1A A:HEM608 3.5 16.6 0.7 C4D A:HEM608 3.5 16.8 1.0 FE A:HEM608 3.6 16.1 1.0 CHA A:HEM608 3.6 16.1 1.0 C4A A:HEM608 4.1 16.3 1.0 NE2 A:GLN105 4.1 12.7 1.0 ND1 A:HIS109 4.1 15.8 1.0 CD A:ARG255 4.1 18.2 1.0 CG A:HIS109 4.2 16.3 1.0 NH1 A:ARG255 4.2 18.7 1.0 C1D A:HEM608 4.2 16.4 1.0 C2A A:HEM608 4.3 17.0 1.0 C3D A:HEM608 4.3 16.7 1.0 O A:HOH974 4.3 19.8 0.7 CG A:GLN105 4.5 13.1 1.0 NB A:HEM608 4.5 16.0 1.0 C3A A:HEM608 4.6 16.2 1.0 NC A:HEM608 4.7 15.8 1.0 C2D A:HEM608 4.7 16.9 1.0 CBD A:HEM608 4.7 18.0 0.7 CHB A:HEM608 4.7 16.1 1.0 NE A:ARG255 4.7 18.1 1.0 CBD A:HEM608 4.8 16.3 0.3 CZ A:ARG255 4.8 18.9 1.0 CD A:GLN105 4.8 12.9 1.0 C1B A:HEM608 4.9 15.5 1.0 OD1 A:ASP108 4.9 26.6 1.0 CHD A:HEM608 5.0 16.3 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution


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 Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:K610 b:14.2 occ:0.70 O A:HOH875 3.3 13.2 1.0 N A:TRP46 3.3 19.0 1.0 N A:VAL342 3.4 16.9 1.0 CH2 A:TRP452 3.7 17.3 1.0 CA A:ARG45 3.8 18.5 1.0 CB A:VAL342 3.8 17.1 1.0 CB A:ASN341 3.8 16.8 1.0 O A:ALA44 3.8 16.9 1.0 N A:ASN341 3.9 15.3 1.0 CG1 A:VAL342 3.9 17.2 1.0 C A:ARG45 4.0 18.9 1.0 CB A:TRP46 4.1 19.3 1.0 CZ2 A:TRP452 4.1 16.7 1.0 CA A:VAL342 4.1 16.7 1.0 CA A:ASN341 4.1 16.4 1.0 N A:LEU47 4.2 17.5 1.0 CE A:MET446 4.2 16.5 1.0 C A:ASN341 4.2 16.8 1.0 CA A:TRP46 4.2 18.5 1.0 CD A:ARG45 4.2 18.1 1.0 CB A:SER340 4.3 14.6 1.0 O A:LEU47 4.3 19.1 1.0 C A:SER340 4.6 14.5 1.0 CG A:TRP46 4.6 20.1 1.0 C A:ALA44 4.6 17.3 1.0 N A:ARG45 4.7 18.1 1.0 CB A:ARG45 4.7 19.0 1.0 C A:TRP46 4.8 18.8 1.0 CA A:SER340 4.8 15.1 1.0 CZ3 A:TRP452 4.8 17.8 1.0 OG A:SER340 4.9 14.9 1.0 NH1 A:ARG45 4.9 18.2 1.0 CG A:ARG45 5.0 18.8 1.0

P.K.Singh, C.Rani, P.Sharma, S.Sharma, T.P.Singh. Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.30 A Resolution To Be Published.