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Manganese in PDB 5ox5: Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound

Enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound

All present enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound:
1.14.11.29;

Protein crystallography data

The structure of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound, PDB code: 5ox5 was solved by R.Chowdhury, C.C.Thinnes, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.69 / 2.25
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 110.147, 110.147, 39.368, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 20.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound (pdb code 5ox5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound, PDB code: 5ox5:

Manganese binding site 1 out of 1 in 5ox5

Go back to Manganese Binding Sites List in 5ox5
Manganese binding site 1 out of 1 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with CCT6, A GSK1278863-Related Compound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:27.2
occ:1.00
 O6 A:B2E502 1.9 29.5 1.0
H6 A:B2E502 2.1 35.5 1.0
OD1 A:ASP315 2.2 38.9 1.0
NE2 A:HIS374 2.2 39.1 1.0
OAN A:B2E502 2.2 29.9 1.0
O A:HOH608 2.2 31.2 1.0
NE2 A:HIS313 2.2 29.3 1.0
CE1 A:HIS313 3.0 28.5 1.0
HE1 A:HIS313 3.1 34.2 1.0
CE1 A:HIS374 3.1 30.6 1.0
C6 A:B2E502 3.1 28.1 1.0
CAJ A:B2E502 3.1 28.1 1.0
CG A:ASP315 3.2 32.1 1.0
CD2 A:HIS374 3.2 31.5 1.0
HE1 A:HIS374 3.2 36.7 1.0
CD2 A:HIS313 3.3 29.4 1.0
HD2 A:HIS374 3.4 37.8 1.0
OD2 A:ASP315 3.5 32.0 1.0
HD2 A:HIS313 3.6 35.3 1.0
C5 A:B2E502 3.6 29.3 1.0
HZ2 A:TRP389 4.1 42.8 1.0
ND1 A:HIS313 4.2 29.7 1.0
ND1 A:HIS374 4.2 32.3 1.0
HZ A:PHE366 4.3 37.5 1.0
O A:HOH619 4.3 28.7 1.0
CG A:HIS374 4.3 30.6 1.0
HA6 A:B2E502 4.3 36.5 1.0
CG A:HIS313 4.3 29.7 1.0
HA A:ASP315 4.3 38.1 1.0
N1 A:B2E502 4.4 29.4 1.0
N A:B2E502 4.4 28.0 1.0
HA1 A:B2E502 4.5 30.6 1.0
CB A:ASP315 4.5 30.8 1.0
HAQ A:B2E502 4.6 36.5 1.0
CAQ A:B2E502 4.7 30.4 1.0
HA2 A:B2E502 4.7 30.6 1.0
CA A:B2E502 4.8 25.5 1.0
CA A:ASP315 4.8 31.7 1.0
HG21 A:THR325 4.8 35.5 1.0
HD1 A:HIS313 4.9 35.6 1.0
H A:ASP315 4.9 38.9 1.0
HD1 A:HIS374 5.0 38.8 1.0
N A:ASP315 5.0 32.4 1.0

Reference:

T.L.Yeh, T.M.Leissing, M.I.Abboud, C.C.Thinnes, O.Atasoylu, J.P.Holt-Martyn, D.Zhang, A.Tumber, K.Lippl, C.T.Lohans, I.K.H.Leung, H.Morcrette, I.J.Clifton, T.D.W.Claridge, A.Kawamura, E.Flashman, X.Lu, P.J.Ratcliffe, R.Chowdhury, C.W.Pugh, C.J.Schofield. Molecular and Cellular Mechanisms of Hif Prolyl Hydroxylase Inhibitors in Clinical Trials. Chem Sci V. 8 7651 2017.
ISSN: ISSN 2041-6520
PubMed: 29435217
DOI: 10.1039/C7SC02103H
Page generated: Sun Oct 6 02:25:32 2024

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