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Arsenic in PDB 2v5c: Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure

Enzymatic activity of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure

All present enzymatic activity of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure:
3.2.1.52;

Protein crystallography data

The structure of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure, PDB code: 2v5c was solved by E.Ficko-Blean, K.J.Gregg, J.J.Adams, J.H.Hehemann, S.J.Smith, M.Czjzek, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 105.41 / 2.10
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 130.385, 150.046, 155.428, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 25.5

Other elements in 2v5c:

The structure of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure also contains other interesting chemical elements:

Calcium (Ca) 4 atoms
Sodium (Na) 2 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure (pdb code 2v5c). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 5 binding sites of Arsenic where determined in the Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure, PDB code: 2v5c:
Jump to Arsenic binding site number: 1; 2; 3; 4; 5;

Arsenic binding site 1 out of 5 in 2v5c

Go back to Arsenic Binding Sites List in 2v5c
Arsenic binding site 1 out of 5 in the Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1627

b:66.7
occ:1.00
AS A:CAC1627 0.0 66.7 1.0
O2 A:CAC1627 1.7 68.2 1.0
O1 A:CAC1627 1.7 68.5 1.0
C2 A:CAC1627 2.0 68.0 1.0
C1 A:CAC1627 2.0 67.3 1.0
OH A:TYR456 3.7 21.4 1.0
O A:HOH2623 3.8 30.4 1.0
O A:HOH2624 3.9 40.6 1.0
CE1 A:HIS413 4.1 14.1 1.0
O A:HOH2464 4.1 31.5 1.0
O A:HOH2423 4.3 51.4 1.0
CZ A:TYR456 4.6 20.6 1.0
NE2 A:HIS413 4.6 15.1 1.0
O A:HOH2421 4.7 26.8 1.0
CE2 A:TYR456 4.8 19.9 1.0
O A:HOH2085 4.8 45.9 1.0
O A:HOH2595 4.9 33.7 1.0

Arsenic binding site 2 out of 5 in 2v5c

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Arsenic binding site 2 out of 5 in the Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1628

b:82.6
occ:1.00
AS A:CAC1628 0.0 82.6 1.0
O1 A:CAC1628 1.7 81.9 1.0
O2 A:CAC1628 1.7 80.8 1.0
C1 A:CAC1628 2.0 81.9 1.0
C2 A:CAC1628 2.0 82.1 1.0
OD1 A:ASP401 3.5 16.1 1.0
OD2 A:ASP401 3.7 18.2 1.0
CG A:ASP401 4.0 17.1 1.0
O A:HOH2371 4.3 30.4 1.0
O A:HOH2074 4.4 38.6 1.0
OD1 A:ASN396 4.5 21.2 1.0
ND2 A:ASN429 4.6 18.3 1.0
O B:LEU623 4.6 35.1 1.0
CD1 A:TYR189 4.7 31.4 1.0
CE1 A:TYR189 4.7 32.6 1.0
CG A:ASN396 4.8 18.1 1.0
ND2 A:ASN396 4.9 17.9 1.0
CG1 A:VAL370 5.0 17.2 1.0

Arsenic binding site 3 out of 5 in 2v5c

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Arsenic binding site 3 out of 5 in the Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1629

b:48.3
occ:1.00
AS A:CAC1629 0.0 48.3 1.0
O2 A:CAC1629 1.7 47.8 1.0
O1 A:CAC1629 1.7 47.8 1.0
C1 A:CAC1629 2.0 48.4 1.0
C2 A:CAC1629 2.0 47.0 1.0
OH A:TYR583 3.4 23.2 1.0
O A:HOH2579 3.9 40.8 1.0
O A:HOH2626 4.2 27.1 1.0
CZ A:TYR583 4.3 23.4 1.0
NZ A:LYS587 4.3 27.0 1.0
CE2 A:TYR583 4.4 22.4 1.0
OD2 A:ASP620 4.5 25.0 1.0
O A:LEU617 4.7 21.4 1.0
CG A:ASP620 4.8 23.4 1.0
O B:HOH2327 4.8 31.3 1.0
O B:HOH2330 4.8 19.0 1.0
NA A:NA1630 4.9 10.4 1.0
CB A:ASP620 4.9 23.1 1.0
O A:PHE619 4.9 22.4 1.0

Arsenic binding site 4 out of 5 in 2v5c

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Arsenic binding site 4 out of 5 in the Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As1627

b:81.7
occ:1.00
AS B:CAC1627 0.0 81.7 1.0
O1 B:CAC1627 1.7 81.8 1.0
O2 B:CAC1627 1.7 81.5 1.0
C1 B:CAC1627 2.0 82.3 1.0
C2 B:CAC1627 2.0 82.1 1.0
OH B:TYR456 3.7 26.7 1.0
O B:HOH2565 3.9 33.6 1.0
O B:HOH2140 4.0 38.0 1.0
O B:HOH2399 4.1 29.2 1.0
CE1 B:HIS413 4.1 16.0 1.0
CZ B:TYR456 4.6 25.5 1.0
CE2 B:TYR456 4.6 26.7 1.0
NE2 B:HIS413 4.8 17.9 1.0
O B:HOH2040 4.9 42.0 1.0
O B:HOH2368 4.9 37.5 1.0

Arsenic binding site 5 out of 5 in 2v5c

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Arsenic binding site 5 out of 5 in the Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 5 of Family 84 Glycoside Hydrolase From Clostridium Perfringens, 2.1 Angstrom Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As1628

b:79.3
occ:1.00
AS B:CAC1628 0.0 79.3 1.0
O2 B:CAC1628 1.7 78.9 1.0
O1 B:CAC1628 1.7 78.3 1.0
C1 B:CAC1628 2.0 79.4 1.0
C2 B:CAC1628 2.0 78.5 1.0
OD1 B:ASP401 3.5 18.4 1.0
OD2 B:ASP401 3.8 17.8 1.0
CG B:ASP401 4.1 18.1 1.0
O B:HOH2265 4.4 38.3 1.0
OD1 B:ASN396 4.4 14.5 1.0
O B:HOH2323 4.5 38.9 1.0
ND2 B:ASN429 4.6 19.7 1.0
CG B:ASN396 4.6 16.4 1.0
ND2 B:ASN396 4.7 17.8 1.0
O A:LEU623 4.8 30.4 1.0
CG1 B:VAL370 4.8 12.6 1.0
CD1 B:TYR189 4.9 31.8 1.0
CG2 B:VAL399 5.0 19.4 1.0

Reference:

E.Ficko-Blean, K.J.Gregg, J.J.Adams, J.H.Hehemann, S.J.Smith, M.Czjzek, A.B.Boraston. Portrait of An Enzyme: A Complete Structural Analysis of A Multi-Modular Beta-N- Acetylglucosaminidase From Clostridium Perfringens J.Biol.Chem. V. 284 9876 2009.
ISSN: ISSN 0021-9258
PubMed: 19193644
DOI: 10.1074/JBC.M808954200
Page generated: Tue Oct 27 16:49:21 2020

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