Atomistry » Magnesium » PDB 6ly3-6m5v » 6ly7
Atomistry »
  Magnesium »
    PDB 6ly3-6m5v »
      6ly7 »

Magnesium in PDB 6ly7: Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp

Enzymatic activity of Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp

All present enzymatic activity of Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp:
6.1.1.26;

Protein crystallography data

The structure of Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp, PDB code: 6ly7 was solved by J.H.Weng, M.D.Tsai, Y.S.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.36 / 2.09
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 105.346, 105.346, 72.396, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / 18.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp (pdb code 6ly7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp, PDB code: 6ly7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6ly7

Go back to Magnesium Binding Sites List in 6ly7
Magnesium binding site 1 out of 2 in the Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:37.7
occ:1.00
OG A:SER399 2.3 45.9 1.0
O2A A:ANP501 2.4 43.5 1.0
O1B A:ANP501 2.4 46.7 1.0
OE1 A:GLU396 2.4 45.7 1.0
HOA2 A:ANP501 2.5 52.2 1.0
OE2 A:GLU396 2.9 55.0 1.0
CD A:GLU396 3.0 47.9 1.0
HNB1 A:ANP501 3.3 57.7 1.0
CB A:SER399 3.4 42.7 1.0
PB A:ANP501 3.4 58.7 1.0
HB2 A:SER399 3.4 51.2 1.0
PA A:ANP501 3.5 41.9 1.0
O A:HOH690 3.6 62.2 1.0
O3A A:ANP501 3.6 42.4 1.0
HB3 A:SER399 3.8 51.2 1.0
N3B A:ANP501 3.8 48.1 1.0
O A:HOH677 4.2 42.7 1.0
O A:HOH605 4.2 49.4 1.0
O1A A:ANP501 4.2 39.4 1.0
OD1 A:ASP389 4.4 53.2 1.0
CG A:GLU396 4.5 44.2 1.0
H3' A:ANP501 4.5 44.9 1.0
H5'1 A:ANP501 4.5 45.8 1.0
CA A:SER399 4.5 44.7 1.0
O3' A:ANP501 4.7 38.7 1.0
HG2 A:GLU396 4.7 53.1 1.0
N A:SER399 4.7 41.8 1.0
H A:SER399 4.7 50.2 1.0
O2B A:ANP501 4.7 46.5 1.0
HA A:SER399 4.8 53.6 1.0
O5' A:ANP501 4.8 44.1 1.0
HOB2 A:ANP501 4.8 55.8 1.0
HG3 A:GLU396 4.8 53.1 1.0

Magnesium binding site 2 out of 2 in 6ly7

Go back to Magnesium Binding Sites List in 6ly7
Magnesium binding site 2 out of 2 in the Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Pylrs C-Terminus Domain Mutant Bound with 1-Formyl-L-Tryptophan and Ampnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:41.1
occ:1.00
O2B A:ANP501 1.9 46.5 1.0
O2G A:ANP501 1.9 40.1 1.0
O A:HOH660 2.0 41.8 1.0
O A:HOH618 2.1 37.5 1.0
HOB2 A:ANP501 2.2 55.8 1.0
O A:HOH674 2.2 41.3 1.0
HOG2 A:ANP501 2.3 48.2 1.0
O A:HOH697 2.3 44.5 1.0
HH21 A:ARG330 3.2 42.6 1.0
PG A:ANP501 3.2 46.4 1.0
PB A:ANP501 3.3 58.7 1.0
HH22 A:ARG330 3.7 42.6 1.0
N3B A:ANP501 3.7 48.1 1.0
NH2 A:ARG330 3.8 35.5 1.0
HE22 A:GLN287 3.9 61.2 1.0
O3G A:ANP501 3.9 43.2 1.0
O1B A:ANP501 4.1 46.7 1.0
O A:HOH733 4.1 54.5 1.0
NE2 A:HIS338 4.1 45.5 1.0
OE2 A:GLU332 4.2 41.1 1.0
HD2 A:HIS338 4.2 48.8 1.0
O A:HOH605 4.3 49.4 1.0
O3A A:ANP501 4.3 42.4 1.0
O1G A:ANP501 4.4 39.2 1.0
HOG3 A:ANP501 4.4 51.9 1.0
OE2 A:GLU283 4.5 76.5 1.0
HNB1 A:ANP501 4.5 57.7 1.0
OE1 A:GLN287 4.5 53.0 1.0
OE1 A:GLU332 4.6 39.5 1.0
CD2 A:HIS338 4.6 40.6 1.0
N7 A:ANP501 4.6 38.0 1.0
HD3 A:ARG330 4.6 45.5 1.0
HD2 A:ARG330 4.7 45.5 1.0
NE2 A:GLN287 4.7 51.0 1.0
CD A:GLU332 4.8 42.5 1.0
H8 A:ANP501 4.8 48.7 1.0
CD A:GLU283 5.0 79.6 1.0

Reference:

H.K.Jiang, Y.H.Wang, J.H.Weng, P.Kurkute, C.L.Li, M.N.Lee, P.J.Chen, H.W.Tseng, M.D.Tsai, Y.S.Wang. Probing the Active Site of Deubiquitinase USP30 with Noncanonical Tryptophan Analogues. Biochemistry V. 59 2205 2020.
ISSN: ISSN 0006-2960
PubMed: 32484330
DOI: 10.1021/ACS.BIOCHEM.0C00307
Page generated: Tue Oct 1 10:47:54 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy