Cobalt in PDB 4p7w: L-Proline-Bound L-Proline Cis-4-Hydroxylase

The structure of L-Proline-Bound L-Proline Cis-4-Hydroxylase, PDB code: 4p7w 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)	19.97 / 1.80
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	55.390, 73.615, 95.045, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 21.6

The binding sites of Cobalt atom in the L-Proline-Bound L-Proline Cis-4-Hydroxylase (pdb code 4p7w). 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-Proline-Bound L-Proline Cis-4-Hydroxylase, PDB code: 4p7w:

Cobalt binding site 1 out of 1 in the L-Proline-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-Proline-Bound L-Proline Cis-4-Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Co301 b:32.5 occ:1.00 OD2 A:ASP108 2.1 34.0 1.0 O2 A:AKG302 2.1 33.0 1.0 NE2 A:HIS106 2.1 35.0 1.0 NE2 A:HIS154 2.1 36.1 1.0 O5 A:AKG302 2.2 32.8 1.0 C2 A:AKG302 2.8 33.8 1.0 C1 A:AKG302 2.8 35.4 1.0 CE1 A:HIS106 3.0 32.7 1.0 CE1 A:HIS154 3.0 37.6 1.0 CG A:ASP108 3.0 33.2 1.0 CD2 A:HIS106 3.2 35.4 1.0 CD2 A:HIS154 3.2 35.4 1.0 OD1 A:ASP108 3.3 32.1 1.0 NH1 A:ARG118 4.0 34.0 1.0 O1 A:AKG302 4.1 35.0 1.0 ND1 A:HIS106 4.1 32.4 1.0 ND1 A:HIS154 4.1 38.4 1.0 CG A:HIS106 4.2 34.5 1.0 C3 A:AKG302 4.3 33.6 1.0 CG A:HIS154 4.3 36.1 1.0 CB A:ASP108 4.3 35.2 1.0 CB A:ALA150 4.4 41.9 1.0 CG A:PRO303 4.6 37.2 1.0 CD1 A:ILE103 4.9 29.8 1.0 N A:ASP108 4.9 36.3 1.0 CD A:PRO303 5.0 37.9 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