Atomistry » Arsenic » PDB 4zt2-5hlo » 5cnx
Atomistry »
  Arsenic »
    PDB 4zt2-5hlo »
      5cnx »

Arsenic in PDB 5cnx: Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12

Protein crystallography data

The structure of Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12, PDB code: 5cnx was solved by A.Kumar, V.Are, B.Ghosh, S.Jamdar, R.D.Makde, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.90 / 2.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 224.202, 224.202, 74.636, 90.00, 90.00, 120.00
R / Rfree (%) 21.9 / 24

Other elements in 5cnx:

The structure of Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12 also contains other interesting chemical elements:

Zinc (Zn) 6 atoms
Sodium (Na) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12 (pdb code 5cnx). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 3 binding sites of Arsenic where determined in the Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12, PDB code: 5cnx:
Jump to Arsenic binding site number: 1; 2; 3;

Arsenic binding site 1 out of 3 in 5cnx

Go back to Arsenic Binding Sites List in 5cnx
Arsenic binding site 1 out of 3 in the Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As403

b:55.7
occ:1.00
AS A:CAC403 0.0 55.7 1.0
O2 A:CAC403 1.7 62.0 1.0
O1 A:CAC403 1.7 46.9 1.0
C2 A:CAC403 2.0 55.3 1.0
C1 A:CAC403 2.0 49.6 1.0
ZN A:ZN401 3.2 44.1 1.0
ZN A:ZN402 3.3 37.6 1.0
OD2 A:ASP223 3.7 41.7 1.0
NE2 A:HIS299 3.7 50.5 1.0
OD2 A:ASP212 4.1 39.1 1.0
NE2 A:HIS292 4.2 41.5 1.0
OD1 A:ASP223 4.2 43.8 1.0
OE1 A:GLU321 4.3 44.5 1.0
OD1 A:ASP212 4.3 38.9 1.0
CE1 A:HIS299 4.3 48.9 1.0
CG A:ASP223 4.3 42.5 1.0
CE1 A:HIS195 4.5 60.8 1.0
CG A:ASP212 4.5 39.4 1.0
OE2 A:GLU321 4.6 41.7 1.0
OE2 A:GLU335 4.7 40.4 1.0
CZ A:PHE181 4.7 33.2 1.0
CE1 A:PHE181 4.7 32.9 1.0
CD2 A:HIS299 4.8 50.1 1.0
OE1 A:GLU335 4.8 40.1 1.0
CD A:GLU321 4.9 42.9 1.0
NE2 A:HIS195 4.9 60.3 1.0
CD2 A:HIS292 4.9 41.7 1.0
CG1 A:VAL298 5.0 32.4 1.0

Arsenic binding site 2 out of 3 in 5cnx

Go back to Arsenic Binding Sites List in 5cnx
Arsenic binding site 2 out of 3 in the Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As403

b:62.6
occ:1.00
AS B:CAC403 0.0 62.6 1.0
O2 B:CAC403 1.7 69.8 1.0
O1 B:CAC403 1.8 59.6 1.0
C2 B:CAC403 2.0 56.7 1.0
C1 B:CAC403 2.0 65.4 1.0
ZN B:ZN401 3.2 42.6 1.0
ZN B:ZN402 3.3 36.7 1.0
NE2 B:HIS299 3.6 45.8 1.0
OD2 B:ASP223 3.6 38.3 1.0
NE2 B:HIS292 4.1 34.2 1.0
OD2 B:ASP212 4.1 38.6 1.0
OE1 B:GLU321 4.2 42.0 1.0
CE1 B:HIS299 4.2 46.2 1.0
OD1 B:ASP223 4.3 37.9 1.0
O B:HOH516 4.3 31.1 1.0
CG B:ASP223 4.4 38.4 1.0
OE2 B:GLU321 4.4 41.8 1.0
OD1 B:ASP212 4.6 38.9 1.0
CG B:ASP212 4.7 38.7 1.0
CD2 B:HIS299 4.7 46.2 1.0
CD B:GLU321 4.7 41.6 1.0
CZ B:PHE181 4.8 33.8 1.0
CE2 B:PHE181 4.8 33.6 1.0
OE2 B:GLU335 4.8 41.4 1.0
CD2 B:HIS292 4.8 34.6 1.0
CE1 B:HIS292 4.9 34.8 1.0
OE1 B:GLU335 4.9 40.0 1.0
CG1 B:VAL298 5.0 40.6 1.0

Arsenic binding site 3 out of 3 in 5cnx

Go back to Arsenic Binding Sites List in 5cnx
Arsenic binding site 3 out of 3 in the Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Crystal Structure of Xaa-Pro Aminopeptidase From Escherichia Coli K12 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As403

b:51.0
occ:0.68
AS C:CAC403 0.0 51.0 0.7
O2 C:CAC403 1.7 45.5 0.7
O1 C:CAC403 1.7 46.6 0.7
C2 C:CAC403 2.0 49.1 0.7
C1 C:CAC403 2.0 47.2 0.7
ZN C:ZN401 3.2 49.8 1.0
ZN C:ZN402 3.4 43.3 1.0
NE2 C:HIS299 3.7 54.9 1.0
OD2 C:ASP223 3.8 44.4 1.0
OD2 C:ASP212 4.0 40.5 1.0
NE2 C:HIS292 4.2 40.2 1.0
OE1 C:GLU321 4.2 49.7 1.0
CE1 C:HIS299 4.3 53.4 1.0
OD1 C:ASP223 4.3 44.3 1.0
OE2 C:GLU321 4.4 50.3 1.0
CG C:ASP223 4.4 45.0 1.0
OD1 C:ASP212 4.5 41.9 1.0
CG C:ASP212 4.6 41.2 1.0
CD C:GLU321 4.8 50.2 1.0
CD2 C:HIS299 4.8 55.0 1.0
CZ C:PHE181 4.8 36.6 1.0
CD2 C:HIS292 4.9 40.2 1.0
CE2 C:PHE181 4.9 34.8 1.0
CE1 C:HIS292 4.9 41.1 1.0
CG1 C:VAL298 5.0 45.1 1.0
OE1 C:GLU335 5.0 53.8 1.0

Reference:

V.N.Are, A.Kumar, V.D.Goyal, S.S.Gotad, B.Ghosh, R.Gadre, S.N.Jamdar, R.D.Makde. Structures and Activities of Widely Conserved Small Prokaryotic Aminopeptidases-P Clarify Classification of M24B Peptidases Proteins 2018.
ISSN: ESSN 1097-0134
PubMed: 30536999
DOI: 10.1002/PROT.25641
Page generated: Sat Dec 12 01:46:28 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy