Chlorine in PDB 8h7t: Trans-3/4-Proline-Hydroxylase H11 Apo Structure

Protein crystallography data

The structure of Trans-3/4-Proline-Hydroxylase H11 Apo Structure, PDB code: 8h7t was solved by W.M.Gong, X.Y.Hu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.78 / 1.88
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 106.6, 106.6, 143.7, 90, 90, 90
R / Rfree (%) 13.3 / 18.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Trans-3/4-Proline-Hydroxylase H11 Apo Structure (pdb code 8h7t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Trans-3/4-Proline-Hydroxylase H11 Apo Structure, PDB code: 8h7t:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 8h7t

Go back to Chlorine Binding Sites List in 8h7t
Chlorine binding site 1 out of 2 in the Trans-3/4-Proline-Hydroxylase H11 Apo Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Trans-3/4-Proline-Hydroxylase H11 Apo Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:40.0
occ:1.00
NH2 A:ARG246 3.3 34.3 1.0
NE2 A:GLN97 3.3 25.1 1.0
NH1 A:ARG246 3.3 36.3 1.0
O A:HOH428 3.4 33.6 1.0
NE1 A:TRP120 3.4 26.4 1.0
CG2 A:THR172 3.7 46.3 1.0
CZ A:ARG246 3.7 32.1 1.0
CD1 A:TRP120 3.9 27.1 1.0
OE1 A:GLN97 3.9 28.4 1.0
CD A:GLN97 4.0 24.7 1.0
CB A:PHE119 4.1 35.4 1.0
N A:THR172 4.3 45.4 1.0
CD2 A:PHE119 4.3 41.7 1.0
OG1 A:THR172 4.4 39.2 1.0
CG A:PHE119 4.4 40.8 1.0
CB A:THR172 4.6 40.5 1.0
CE2 A:TRP120 4.6 24.8 1.0
CA A:ASN171 4.8 63.5 1.0
C A:ASN171 5.0 56.2 1.0

Chlorine binding site 2 out of 2 in 8h7t

Go back to Chlorine Binding Sites List in 8h7t
Chlorine binding site 2 out of 2 in the Trans-3/4-Proline-Hydroxylase H11 Apo Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Trans-3/4-Proline-Hydroxylase H11 Apo Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl301

b:40.1
occ:1.00
O B:HOH452 3.2 35.4 1.0
NH2 B:ARG246 3.2 36.4 1.0
NE2 B:GLN97 3.3 23.7 1.0
NH1 B:ARG246 3.3 33.6 1.0
NE1 B:TRP120 3.4 27.4 1.0
CZ B:ARG246 3.7 35.6 1.0
CG2 B:THR172 3.8 52.3 1.0
CD1 B:TRP120 3.9 26.1 1.0
OE1 B:GLN97 3.9 29.9 1.0
CD B:GLN97 4.0 24.4 1.0
CB B:PHE119 4.0 31.2 1.0
CD2 B:PHE119 4.2 42.2 1.0
CG B:PHE119 4.3 37.8 1.0
N B:THR172 4.4 45.9 1.0
OG1 B:THR172 4.5 47.8 1.0
CE2 B:TRP120 4.6 24.4 1.0
CB B:THR172 4.7 49.4 1.0
CA B:ASN171 4.8 55.1 1.0

Reference:

X.Hu, X.Huang, J.Liu, P.Zheng, W.Gong, L.Yang. Structures of L-Proline Trans-Hydroxylase Reveal the Catalytic Specificity and Provide Deeper Insight Into Akg-Dependent Hydroxylation. Acta Crystallogr D Struct V. 79 318 2023BIOL.
ISSN: ISSN 2059-7983
PubMed: 36974966
DOI: 10.1107/S2059798323001936
Page generated: Tue Jul 30 10:16:18 2024

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