Cobalt in PDB 4p7x: L-Pipecolic Acid-Bound L-Proline Cis-4-Hydroxylase

The structure of L-Pipecolic Acid-Bound L-Proline Cis-4-Hydroxylase, PDB code: 4p7x was solved by Y.Shomura, K.Koketsu, K.Moriwaki, M.Hayashi, S.Mitsuhashi, R.Hara, K.Kino, Y.Higuchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.87 / 1.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	112.680, 123.395, 56.980, 90.00, 90.00, 90.00
R / Rfree (%)	13.5 / 16.2

The binding sites of Cobalt atom in the L-Pipecolic Acid-Bound L-Proline Cis-4-Hydroxylase (pdb code 4p7x). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the L-Pipecolic Acid-Bound L-Proline Cis-4-Hydroxylase, PDB code: 4p7x:

Cobalt binding site 1 out of 1 in the L-Pipecolic Acid-Bound L-Proline Cis-4-Hydroxylase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of L-Pipecolic Acid-Bound L-Proline Cis-4-Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Co301 b:13.8 occ:1.00 O1 A:AKG302 2.0 16.0 1.0 OD2 A:ASP108 2.0 16.2 1.0 NE2 A:HIS154 2.1 13.8 1.0 O5 A:AKG302 2.1 19.1 1.0 NE2 A:HIS106 2.1 13.8 1.0 C1 A:AKG302 2.8 16.3 1.0 C2 A:AKG302 2.8 18.1 1.0 CG A:ASP108 2.9 14.2 1.0 CE1 A:HIS154 3.0 14.7 1.0 CE1 A:HIS106 3.0 14.3 1.0 OD1 A:ASP108 3.1 16.5 1.0 CD2 A:HIS154 3.2 13.8 1.0 CD2 A:HIS106 3.2 14.7 1.0 O2 A:AKG302 4.0 19.6 1.0 NH1 A:ARG118 4.1 15.4 1.0 ND1 A:HIS154 4.1 13.6 1.0 ND1 A:HIS106 4.1 13.6 1.0 CG A:HIS154 4.2 13.0 1.0 CG A:HIS106 4.3 13.9 1.0 C3 A:AKG302 4.3 17.4 1.0 CB A:ASP108 4.3 14.1 1.0 CB A:ALA150 4.5 15.6 1.0 CD A:YCP303 4.6 17.8 1.0 N A:ASP108 4.8 14.8 1.0 CD1 A:ILE103 4.9 15.6 1.0

K.Koketsu, Y.Shomura, K.Moriwaki, M.Hayashi, S.Mitsuhashi, R.Hara, K.Kino, Y.Higuchi. Refined Regio- and Stereoselective Hydroxylation of L-Pipecolic Acid By Protein Engineering of L-Proline Cis-4-Hydroxylase Based on the X-Ray Crystal Structure. Acs Synth Biol 2014.
ISSN: ESSN 2161-5063
PubMed: 25171735
DOI: 10.1021/SB500247A