Calcium in PDB 8jqp: Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate

The structure of Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate, PDB code: 8jqp was solved by R.Fukushima, N.Katsuki, S.Fushinobu, N.Takaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.52 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.966, 65.074, 80.681, 90, 107.55, 90
R / Rfree (%)	18.2 / 22.1

The binding sites of Calcium atom in the Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate (pdb code 8jqp). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate, PDB code: 8jqp:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca405 b:17.3 occ:1.00 OD2 B:ASP230 2.4 17.1 1.0 OD2 A:ASP134 2.4 16.7 1.0 O A:HOH542 2.5 18.1 1.0 O A:HOH514 2.5 17.6 1.0 OD1 A:ASP134 2.7 18.6 1.0 CG A:ASP134 2.9 20.2 1.0 CG B:ASP230 3.3 14.2 1.0 CB B:ASP230 3.5 12.4 1.0 OD1 A:ASP135 4.0 26.1 1.0 O B:HOH532 4.0 19.2 1.0 OD2 A:ASP135 4.4 26.7 1.0 CB A:ASP134 4.4 16.9 1.0 O A:HOH621 4.5 24.5 1.0 CG A:ASP135 4.5 31.4 1.0 OD1 B:ASP230 4.5 13.2 1.0 O A:HOH603 4.5 17.9 1.0 NH1 A:ARG138 4.5 17.6 1.0 O B:HOH743 4.6 25.8 1.0

Calcium binding site 2 out of 2 in the Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Protocatecuate Hydroxylase From Xylophilus Ampelinus Complexed with 3, 4-Dihydroxybenzoate within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca405 b:15.2 occ:0.95 O B:HOH708 2.4 17.6 1.0 OD2 B:ASP237 2.4 16.6 1.0 OD1 B:ASP237 2.6 15.4 1.0 CG B:ASP237 2.8 16.0 1.0 O B:HOH501 3.9 7.9 1.0 CB B:ASP237 4.3 14.9 1.0 O B:ASP237 4.5 15.2 1.0 CB B:SER241 4.8 17.7 1.0 C B:ASP237 5.0 15.8 1.0

N.Katsuki, R.Fukushima, Y.Doi, S.Masuo, T.Arakawa, C.Yamada, S.Fushinobu, N.Takaya. Protocatechuate Hydroxylase Is A Novel Group A Flavoprotein Monooxygenase with A Unique Substrate Recognition Mechanism. J.Biol.Chem. 05508 2023.
ISSN: ESSN 1083-351X
PubMed: 38029967
DOI: 10.1016/J.JBC.2023.105508