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Bromine in PDB 6yvz: Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367

Enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367

All present enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367:
1.14.11.29;

Protein crystallography data

The structure of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367, PDB code: 6yvz was solved by R.Chowdhury, J.L.Sorensen, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.15 / 1.91
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 109.88, 109.88, 39.08, 90, 90, 120
R / Rfree (%) 16.7 / 20.4

Other elements in 6yvz:

The structure of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367 also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367 (pdb code 6yvz). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367, PDB code: 6yvz:

Bromine binding site 1 out of 1 in 6yvz

Go back to Bromine Binding Sites List in 6yvz
Bromine binding site 1 out of 1 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Bicyclic Jls- 367 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br502

b:120.5
occ:1.00
 BR1 A:PW8502 0.0 120.5 1.0
C10 A:PW8502 2.0 130.9 1.0
H081 A:PW8502 2.7 98.3 1.0
C12 A:PW8502 2.9 126.6 1.0
C09 A:PW8502 2.9 102.9 1.0
H121 A:PW8502 3.0 152.0 1.0
C08 A:PW8502 3.2 81.9 1.0
HE2 A:TYR310 3.4 59.8 1.0
HD13 A:ILE256 3.5 65.2 1.0
O A:HOH607 3.5 52.2 1.0
HG21 A:ILE256 3.7 67.2 1.0
OD2 A:ASP254 3.9 46.8 1.0
OH A:TYR310 4.0 49.9 1.0
O A:HOH642 4.0 88.2 1.0
SD A:MET299 4.1 61.0 0.4
CE2 A:TYR310 4.2 49.7 1.0
C15 A:PW8502 4.2 94.0 1.0
C13 A:PW8502 4.2 117.1 1.0
HG23 A:ILE256 4.3 67.2 1.0
SD A:MET299 4.4 61.0 0.6
CG2 A:ILE256 4.4 55.9 1.0
CD1 A:ILE256 4.4 54.3 1.0
CZ A:TYR310 4.5 47.8 1.0
C07 A:PW8502 4.6 62.8 1.0
HD12 A:ILE256 4.6 65.2 1.0
HH A:TYR310 4.7 59.9 1.0
C14 A:PW8502 4.8 106.9 1.0
HD11 A:ILE256 4.9 65.2 1.0
O A:HOH641 4.9 31.6 1.0
H131 A:PW8502 4.9 140.6 1.0
HG22 A:ILE256 5.0 67.2 1.0

Reference:

R.Chowdhury, M.I.Abboud, T.E.Mcallister, B.Banerji, B.Bhushan, J.L.Sorensen, A.Kawamura, C.J.Schofield. Use of Cyclic Peptides to Induce Crystallization: Case Study with Prolyl Hydroxylase Domain 2. Sci Rep V. 10 21964 2020.
ISSN: ESSN 2045-2322
PubMed: 33319810
DOI: 10.1038/S41598-020-76307-8
Page generated: Mon Jul 7 10:47:22 2025

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