Atomistry » Bromine » PDB 4alv-4d46 » 4brp
Atomistry »
  Bromine »
    PDB 4alv-4d46 »
      4brp »

Bromine in PDB 4brp: Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)

Enzymatic activity of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)

All present enzymatic activity of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open):
3.6.1.5;

Protein crystallography data

The structure of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open), PDB code: 4brp was solved by M.Zebisch, P.Schaefer, P.Lauble, N.Straeter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.08 / 2.50
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 129.608, 129.608, 162.698, 90.00, 90.00, 120.00
R / Rfree (%) 17.711 / 21.866

Bromine Binding Sites:

The binding sites of Bromine atom in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) (pdb code 4brp). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 7 binding sites of Bromine where determined in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open), PDB code: 4brp:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7;

Bromine binding site 1 out of 7 in 4brp

Go back to Bromine Binding Sites List in 4brp
Bromine binding site 1 out of 7 in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1393

b:93.3
occ:1.00
 ND2 A:ASN327 3.7 86.8 1.0
NE2 A:GLN328 3.8 87.9 1.0
CG A:GLN324 3.8 57.5 1.0
CA A:GLN324 3.9 57.7 1.0
CB A:ASN327 4.0 76.0 1.0
CB A:GLN324 4.3 55.7 1.0
CG A:ASN327 4.4 78.9 1.0
N A:GLN324 4.4 56.7 1.0
O A:GLN323 4.4 62.4 1.0
CG A:GLN323 4.5 72.2 1.0
CG A:GLN328 4.5 75.2 1.0
CD A:GLN328 4.6 85.2 1.0
C A:GLN323 4.6 60.7 1.0
O A:GLN324 4.8 56.0 1.0
C A:GLN324 4.9 55.8 1.0
CD A:GLN324 4.9 59.3 1.0

Bromine binding site 2 out of 7 in 4brp

Go back to Bromine Binding Sites List in 4brp
Bromine binding site 2 out of 7 in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1394

b:49.5
occ:1.00
 CA A:ASP253 3.7 54.8 1.0
N A:ASP253 3.7 51.3 1.0
N B:GLY156 3.7 52.0 1.0
CD B:ARG122 3.8 49.9 1.0
CB A:ASP253 3.8 58.5 1.0
ND2 A:ASN240 3.8 44.4 1.0
C A:PRO252 3.8 47.2 1.0
NE B:ARG122 3.9 51.6 1.0
O A:PRO252 4.0 45.2 1.0
CB A:PRO252 4.1 40.8 1.0
CA B:GLY156 4.4 51.9 1.0
CB B:THR155 4.5 45.2 1.0
CA B:THR155 4.5 44.7 1.0
OD1 A:ASN240 4.6 48.6 1.0
CA A:PRO252 4.6 42.0 1.0
CZ B:ARG122 4.6 50.0 1.0
C B:THR155 4.6 44.8 1.0
CG A:ASN240 4.7 46.7 1.0
CD2 B:LEU227 4.7 42.0 1.0
CB B:SER225 4.8 45.0 1.0
CB B:LEU227 4.9 41.0 1.0

Bromine binding site 3 out of 7 in 4brp

Go back to Bromine Binding Sites List in 4brp
Bromine binding site 3 out of 7 in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br1392

b:52.2
occ:1.00
 N A:GLY156 3.5 45.8 1.0
ND2 B:ASN240 3.6 55.2 1.0
CA B:ASP253 3.7 55.8 1.0
N B:ASP253 3.7 54.9 1.0
CD A:ARG122 3.7 54.1 1.0
CB B:ASP253 3.9 55.9 1.0
C B:PRO252 3.9 52.9 1.0
NE A:ARG122 3.9 56.8 1.0
O B:PRO252 3.9 51.8 1.0
CB B:PRO252 4.2 48.6 1.0
CA A:GLY156 4.2 44.8 1.0
C A:THR155 4.5 43.9 1.0
CA A:THR155 4.5 45.7 1.0
CB A:THR155 4.5 45.6 1.0
CG B:ASN240 4.6 56.9 1.0
CD2 A:LEU227 4.7 49.1 1.0
CA B:PRO252 4.7 51.7 1.0
OD1 B:ASN240 4.7 57.1 1.0
CB A:SER225 4.8 46.1 1.0
CZ A:ARG122 4.8 54.9 1.0
CB A:LEU227 4.9 41.8 1.0

Bromine binding site 4 out of 7 in 4brp

Go back to Bromine Binding Sites List in 4brp
Bromine binding site 4 out of 7 in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br1393

b:0.1
occ:1.00
 ND2 B:ASN327 3.5 83.3 1.0
NE2 B:GLN328 3.7 0.6 1.0
CB B:ASN327 3.8 81.2 1.0
CA B:GLN324 4.0 69.4 1.0
CG B:GLN324 4.1 73.3 1.0
CG B:ASN327 4.1 81.8 1.0
O B:GLN323 4.2 76.4 1.0
CG B:GLN323 4.3 83.2 1.0
N B:GLN324 4.4 70.3 1.0
C B:GLN323 4.5 73.1 1.0
CD B:GLN328 4.5 0.7 1.0
CG B:GLN328 4.6 93.5 1.0
CB B:GLN324 4.6 70.4 1.0
O B:GLN324 4.9 67.5 1.0
CD B:GLN323 4.9 90.5 1.0
C B:GLN324 5.0 66.5 1.0

Bromine binding site 5 out of 7 in 4brp

Go back to Bromine Binding Sites List in 4brp
Bromine binding site 5 out of 7 in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Br1394

b:0.1
occ:1.00
 ND2 C:ASN327 3.5 64.7 1.0
CG C:GLN324 3.7 56.1 1.0
CA C:GLN324 3.8 57.2 1.0
NE2 C:GLN328 3.9 80.4 1.0
CB C:ASN327 4.1 63.6 1.0
O C:GLN323 4.1 63.5 1.0
N C:GLN324 4.3 56.2 1.0
CG C:ASN327 4.3 62.4 1.0
CB C:GLN324 4.3 56.7 1.0
CG C:GLN323 4.3 82.9 1.0
C C:GLN323 4.4 61.2 1.0
CG C:GLN328 4.7 65.7 1.0
CD C:GLN328 4.8 73.5 1.0
CD C:GLN324 4.8 56.5 1.0
C C:GLN324 4.9 53.5 1.0
O C:GLN324 4.9 60.1 1.0
CD C:GLN323 5.0 91.8 1.0

Bromine binding site 6 out of 7 in 4brp

Go back to Bromine Binding Sites List in 4brp
Bromine binding site 6 out of 7 in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Br1395

b:44.1
occ:1.00
 N D:GLY156 3.5 37.2 1.0
N C:ASP253 3.7 36.9 1.0
CD D:ARG122 3.7 44.0 1.0
ND2 C:ASN240 3.8 42.7 1.0
CA C:ASP253 3.8 42.7 1.0
NE D:ARG122 3.8 46.0 1.0
C C:PRO252 3.9 37.6 1.0
O C:PRO252 4.0 39.5 1.0
CB C:ASP253 4.0 44.9 1.0
CB C:PRO252 4.1 36.0 1.0
CA D:GLY156 4.2 36.8 1.0
CA D:THR155 4.4 31.3 1.0
CB D:THR155 4.4 33.0 1.0
C D:THR155 4.4 30.9 1.0
OD1 C:ASN240 4.6 46.5 1.0
CG C:ASN240 4.6 41.0 1.0
CZ D:ARG122 4.7 46.8 1.0
CA C:PRO252 4.7 35.6 1.0
CD2 D:LEU227 4.8 40.6 1.0
O D:HOH2006 4.8 53.3 1.0
CB D:SER225 4.9 43.5 1.0
CB D:LEU227 5.0 37.9 1.0

Bromine binding site 7 out of 7 in 4brp

Go back to Bromine Binding Sites List in 4brp
Bromine binding site 7 out of 7 in the Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 7 of Legionella Pneumophila NTPDASE1 Crystal Form V (Part-Open) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Br1393

b:60.2
occ:1.00
 N C:GLY156 3.5 52.5 1.0
ND2 D:ASN240 3.6 62.0 1.0
CA D:ASP253 3.6 66.2 1.0
N D:ASP253 3.6 64.5 1.0
CB D:ASP253 3.7 67.7 1.0
CD C:ARG122 3.8 58.0 1.0
C D:PRO252 3.9 64.0 1.0
O D:PRO252 4.1 64.6 1.0
NE C:ARG122 4.2 57.2 1.0
CA C:GLY156 4.2 50.0 1.0
CB D:PRO252 4.3 62.3 1.0
CB C:THR155 4.4 59.3 1.0
CA C:THR155 4.4 55.9 1.0
C C:THR155 4.5 53.2 1.0
CG D:ASN240 4.5 64.6 1.0
OD1 D:ASN240 4.5 67.2 1.0
CD2 C:LEU227 4.8 50.1 1.0
CA D:PRO252 4.8 63.6 1.0
CB C:SER225 4.9 48.3 1.0
CZ C:ARG122 4.9 59.5 1.0
CG D:ASP253 5.0 75.6 1.0
CB C:LEU227 5.0 45.9 1.0

Reference:

M.Zebisch, M.Krauss, P.Schaefer, P.Lauble, N.Straeter. Crystallographic Snapshots Along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases Structure V. 21 1460 2013.
ISSN: ISSN 0969-2126
PubMed: 23830739
DOI: 10.1016/J.STR.2013.05.016
Page generated: Wed Jul 10 20:53:37 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