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Lutetium in PDB 7zu8: Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4.

Enzymatic activity of Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4.

All present enzymatic activity of Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4.:
3.4.21.19;

Protein crystallography data

The structure of Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4., PDB code: 7zu8 was solved by L.Del Amo-Maestro, U.Eckhard, A.Rodriguez-Banqueri, S.R.Mendes, T.Guevara, F.X.Gomis-Ruth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.51 / 2.05
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.65, 93.35, 48.69, 90, 90, 90
R / Rfree (%) 20.9 / 25

Lutetium Binding Sites:

The binding sites of Lutetium atom in the Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4. (pdb code 7zu8). This binding sites where shown within 5.0 Angstroms radius around Lutetium atom.
In total 2 binding sites of Lutetium where determined in the Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4., PDB code: 7zu8:
Jump to Lutetium binding site number: 1; 2;

Lutetium binding site 1 out of 2 in 7zu8

Go back to Lutetium Binding Sites List in 7zu8
Lutetium binding site 1 out of 2 in the Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4.


Mono view


Stereo pair view

A full contact list of Lutetium with other atoms in the Lu binding site number 1 of Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Lu501

b:51.7
occ:0.61
LU1 A:K93501 0.0 51.7 0.6
O A:ACT502 2.4 35.7 0.6
OXT A:ACT502 2.4 36.0 0.6
O25 A:K93501 2.4 35.8 0.6
O28 A:K93501 2.4 35.8 0.6
N23 A:K93501 2.5 35.6 0.6
N09 A:K93501 2.5 35.2 0.6
N17 A:K93501 2.5 35.9 0.6
N02 A:K93501 2.6 35.6 0.6
N06 A:K93501 2.6 35.9 0.6
C03 A:K93501 2.7 35.2 0.6
C A:ACT502 2.7 35.9 0.6
C01 A:K93501 3.2 35.4 0.6
C24 A:K93501 3.3 36.1 0.6
C18 A:K93501 3.3 35.8 0.6
C22 A:K93501 3.3 35.5 0.6
C16 A:K93501 3.4 35.9 0.6
C29 A:K93501 3.4 35.1 0.6
C07 A:K93501 3.4 35.7 0.6
C11 A:K93501 3.4 35.1 0.6
C10 A:K93501 3.5 35.8 0.6
C08 A:K93501 3.5 35.3 0.6
C04 A:K93501 3.5 35.9 0.6
C30 A:K93501 3.5 35.8 0.6
C05 A:K93501 3.5 36.0 0.6
CH3 A:ACT502 4.3 36.1 0.6
O26 A:K93501 4.5 37.1 0.6
O27 A:K93501 4.5 35.6 0.6
C21 A:K93501 4.7 35.3 0.6
C15 A:K93501 4.7 35.7 0.6
C19 A:K93501 4.7 35.0 0.6
OG A:SER367 4.8 57.4 1.0
C13 A:K93501 4.8 35.6 0.6
N A:SER367 4.9 51.6 1.0

Lutetium binding site 2 out of 2 in 7zu8

Go back to Lutetium Binding Sites List in 7zu8
Lutetium binding site 2 out of 2 in the Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4.


Mono view


Stereo pair view

A full contact list of Lutetium with other atoms in the Lu binding site number 2 of Crystal Structure of the Zymogen Form of the Glutamic-Class Prolyl- Endopeptidase Neprosin at 2.05 A Resolution in Presence of the Crystallophore Lu-XO4. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Lu503

b:56.9
occ:0.49
LU1 A:K93503 0.0 56.9 0.5
OE2 A:GLU89 2.4 70.0 1.0
OE1 A:GLU89 2.4 67.0 1.0
O25 A:K93503 2.4 42.4 0.5
O28 A:K93503 2.4 41.8 0.5
N23 A:K93503 2.5 41.4 0.5
N17 A:K93503 2.5 41.5 0.5
N06 A:K93503 2.6 41.2 0.5
N09 A:K93503 2.6 41.6 0.5
N02 A:K93503 2.6 41.3 0.5
CD A:GLU89 2.7 66.4 1.0
C07 A:K93503 3.2 41.5 0.5
C03 A:K93503 3.3 41.4 0.5
C24 A:K93503 3.3 41.5 0.5
C18 A:K93503 3.3 41.3 0.5
C22 A:K93503 3.3 41.4 0.5
C16 A:K93503 3.3 41.4 0.5
C11 A:K93503 3.4 41.4 0.5
C29 A:K93503 3.4 41.6 0.5
C10 A:K93503 3.4 41.6 0.5
C30 A:K93503 3.5 41.4 0.5
C08 A:K93503 3.5 41.7 0.5
C04 A:K93503 3.5 41.1 0.5
C01 A:K93503 3.5 41.4 0.5
C05 A:K93503 3.6 41.4 0.5
CG A:GLU89 4.2 59.2 1.0
O26 A:K93503 4.5 40.9 0.5
O27 A:K93503 4.5 41.2 0.5
C21 A:K93503 4.7 41.4 0.5
C15 A:K93503 4.7 41.5 0.5
C19 A:K93503 4.7 41.3 0.5
N A:GLU89 4.8 54.4 1.0
C13 A:K93503 4.8 41.4 0.5
O A:LYS87 4.8 62.9 1.0
O A:HOH683 4.8 40.4 1.0
CB A:GLU89 5.0 54.9 1.0

Reference:

L.Del Amo-Maestro, S.R.Mendes, A.Rodriguez-Banqueri, L.Garzon-Flores, M.Girbal, M.J.Rodriguez-Lagunas, T.Guevara, A.Franch, F.J.Perez-Cano, U.Eckhard, F.X.Gomis-Ruth. Molecular and in Vivo Studies of A Glutamate-Class Prolyl-Endopeptidase For Coeliac Disease Therapy. Nat Commun V. 13 4446 2022.
ISSN: ESSN 2041-1723
PubMed: 35915115
DOI: 10.1038/S41467-022-32215-1
Page generated: Wed Apr 5 10:49:16 2023

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