Atomistry » Manganese » PDB 1xif-1ytm » 1yny
Atomistry »
  Manganese »
    PDB 1xif-1ytm »
      1yny »

Manganese in PDB 1yny: Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition

Enzymatic activity of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition

All present enzymatic activity of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition:
3.5.2.2;

Protein crystallography data

The structure of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition, PDB code: 1yny was solved by K.V.Radha Kishan, R.M.Vohra, K.Ganeshan, V.Agrawal, V.M.Sharma, R.Sharma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.30
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 129.540, 129.540, 102.850, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 24.3

Manganese Binding Sites:

The binding sites of Manganese atom in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition (pdb code 1yny). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition, PDB code: 1yny:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1yny

Go back to Manganese Binding Sites List in 1yny
Manganese binding site 1 out of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn471

b:18.0
occ:1.00
 NE2 A:HIS58 2.1 17.5 1.0
O A:HOH1128 2.1 12.1 1.0
NE2 A:HIS60 2.2 21.1 1.0
OD1 A:ASP315 2.3 14.2 1.0
CE1 A:HIS58 3.0 16.3 1.0
CD2 A:HIS58 3.1 16.0 1.0
CE1 A:HIS60 3.2 18.6 1.0
CD2 A:HIS60 3.2 18.4 1.0
CG A:ASP315 3.2 15.3 1.0
NZ A:LYS150 3.3 12.3 1.0
MN A:MN472 3.4 17.8 1.0
OD2 A:ASP315 3.7 12.8 1.0
O A:HOH1112 3.9 18.5 1.0
O A:HOH1093 4.0 22.7 1.0
ND1 A:HIS58 4.2 15.6 1.0
CG A:HIS58 4.2 15.5 1.0
ND1 A:HIS60 4.3 17.5 1.0
CG A:HIS60 4.3 18.4 1.0
CB A:ASP315 4.3 14.7 1.0
CD2 A:HIS239 4.4 15.8 1.0
CE2 A:PHE92 4.5 11.1 1.0
NE2 A:HIS239 4.5 14.7 1.0
CD2 A:PHE92 4.6 11.7 1.0
CA A:ASP315 4.8 15.2 1.0
CE A:LYS150 4.8 15.0 1.0

Manganese binding site 2 out of 4 in 1yny

Go back to Manganese Binding Sites List in 1yny
Manganese binding site 2 out of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn472

b:17.8
occ:1.00
 O A:HOH1128 2.1 12.1 1.0
ND1 A:HIS183 2.3 15.4 1.0
NE2 A:HIS239 2.3 14.7 1.0
O A:HOH1112 2.5 18.5 1.0
CE1 A:HIS183 3.0 16.9 1.0
CD2 A:HIS239 3.2 15.8 1.0
CE1 A:HIS239 3.3 14.9 1.0
CG A:HIS183 3.4 15.1 1.0
NZ A:LYS150 3.4 12.3 1.0
MN A:MN471 3.4 18.0 1.0
CB A:HIS183 3.8 10.6 1.0
O A:SER288 3.9 14.1 1.0
OH A:TYR155 4.1 17.5 1.0
NE2 A:HIS183 4.2 17.0 1.0
CE A:LYS150 4.3 15.0 1.0
CE2 A:PHE152 4.4 15.5 1.0
CD2 A:HIS183 4.4 16.3 1.0
CG A:HIS239 4.4 16.2 1.0
ND1 A:HIS239 4.4 15.9 1.0
CG2 A:VAL238 4.6 11.3 1.0
CE1 A:HIS58 4.6 16.3 1.0
NE2 A:HIS58 4.6 17.5 1.0
OD2 A:ASP315 4.7 12.8 1.0
O A:HOH1093 4.7 22.7 1.0
CA A:HIS183 4.7 10.5 1.0
CE2 A:TYR155 4.8 21.4 1.0
OD1 A:ASP315 4.9 14.2 1.0
CD2 A:PHE152 4.9 14.4 1.0
CZ A:TYR155 5.0 18.9 1.0
C A:SER288 5.0 14.2 1.0

Manganese binding site 3 out of 4 in 1yny

Go back to Manganese Binding Sites List in 1yny
Manganese binding site 3 out of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn471

b:17.1
occ:1.00
 O B:HOH5110 2.1 19.3 1.0
NE2 B:HIS58 2.2 18.2 1.0
NE2 B:HIS60 2.2 17.1 1.0
OD1 B:ASP315 2.3 14.2 1.0
CD2 B:HIS58 3.1 17.9 1.0
CD2 B:HIS60 3.1 15.2 1.0
NZ B:LYS150 3.2 11.6 1.0
CE1 B:HIS58 3.3 17.4 1.0
CE1 B:HIS60 3.3 16.9 1.0
CG B:ASP315 3.3 14.0 1.0
MN B:MN472 3.5 15.3 1.0
OD2 B:ASP315 3.8 14.6 1.0
O B:HOH5109 4.0 31.0 1.0
O B:HOH5084 4.0 20.2 1.0
CG B:HIS58 4.3 14.6 1.0
CG B:HIS60 4.3 16.4 1.0
ND1 B:HIS58 4.3 15.6 1.0
ND1 B:HIS60 4.3 18.0 1.0
CE2 B:PHE92 4.4 10.8 1.0
CB B:ASP315 4.4 13.3 1.0
CD2 B:HIS239 4.4 12.1 1.0
CD2 B:PHE92 4.5 12.2 1.0
NE2 B:HIS239 4.6 10.1 1.0
CA B:ASP315 4.7 14.1 1.0
CE B:LYS150 4.7 16.6 1.0

Manganese binding site 4 out of 4 in 1yny

Go back to Manganese Binding Sites List in 1yny
Manganese binding site 4 out of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn472

b:15.3
occ:1.00
 O B:HOH5110 2.1 19.3 1.0
ND1 B:HIS183 2.3 11.9 1.0
O B:HOH5109 2.3 31.0 1.0
NE2 B:HIS239 2.3 10.1 1.0
CE1 B:HIS183 3.1 11.4 1.0
CD2 B:HIS239 3.3 12.1 1.0
CE1 B:HIS239 3.3 10.6 1.0
NZ B:LYS150 3.4 11.6 1.0
CG B:HIS183 3.4 12.7 1.0
MN B:MN471 3.5 17.1 1.0
CB B:HIS183 3.8 11.6 1.0
O B:SER288 3.9 15.7 1.0
CE2 B:PHE152 4.2 14.5 1.0
NE2 B:HIS183 4.3 11.6 1.0
OH B:TYR155 4.3 21.5 1.0
CE B:LYS150 4.3 16.6 1.0
CD2 B:HIS183 4.4 13.3 1.0
CG B:HIS239 4.4 13.1 1.0
ND1 B:HIS239 4.4 13.1 1.0
CG2 B:VAL238 4.5 9.5 1.0
NE2 B:HIS58 4.6 18.2 1.0
CE1 B:HIS58 4.7 17.4 1.0
OD2 B:ASP315 4.7 14.6 1.0
CA B:HIS183 4.8 10.5 1.0
O B:HOH5084 4.8 20.2 1.0
OD1 B:ASP315 4.8 14.2 1.0
CE2 B:TYR155 4.9 23.6 1.0
CD2 B:PHE152 4.9 15.7 1.0

Reference:

K.V.Radha Kishan, R.M.Vohra, K.Ganesan, V.Agrawal, V.M.Sharma, R.Sharma. Molecular Structure of D-Hydantoinase From Bacillus Sp. AR9: Evidence For Mercury Inhibition. J.Mol.Biol. V. 347 95 2005.
ISSN: ISSN 0022-2836
PubMed: 15733920
DOI: 10.1016/J.JMB.2005.01.025
Page generated: Sat Oct 5 13:13:17 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