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Arsenic in PDB 1pqu: Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate

Enzymatic activity of Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate

All present enzymatic activity of Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate:
1.2.1.11;

Protein crystallography data

The structure of Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate, PDB code: 1pqu was solved by J.Blanco, R.A.Moore, R.E.Viola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.65 / 1.92
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.929, 76.579, 134.097, 90.00, 92.59, 90.00
R / Rfree (%) 18.2 / 23.4

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate (pdb code 1pqu). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate, PDB code: 1pqu:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in 1pqu

Go back to Arsenic Binding Sites List in 1pqu
Arsenic binding site 1 out of 4 in the Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate


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 the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1375

b:77.1
occ:1.00
AS A:CAC1375 0.0 77.1 1.0
O2 A:CAC1375 1.8 75.1 1.0
O1 A:CAC1375 1.8 75.0 1.0
C2 A:CAC1375 2.0 73.2 1.0
C1 A:CAC1375 2.0 74.1 1.0
NH1 A:ARG103 3.5 12.2 1.0
NH2 A:ARG103 3.6 14.1 1.0
NZ A:LYS246 3.6 22.1 1.0
ND2 A:ASN135 3.8 13.9 1.0
O A:HOH1440 4.0 24.4 1.0
CZ A:ARG103 4.0 13.4 1.0
N A:CYS1374 4.0 30.5 1.0
O A:HOH1393 4.1 39.5 1.0
CA A:ASN135 4.4 12.2 1.0
CB A:SER100 4.5 11.8 1.0
O A:HOH1560 4.6 35.8 1.0
CB A:CYS1374 4.7 30.9 1.0
CG A:ASN135 4.7 16.3 1.0
CB A:ASN135 4.7 13.9 1.0
CE A:LYS246 4.8 23.0 1.0
C6N A:NAP1372 4.8 25.1 1.0
O2D A:NAP1372 4.9 16.1 1.0
CA A:CYS1374 4.9 31.8 1.0
CD A:LYS246 5.0 20.2 1.0
OG A:SER100 5.0 10.9 1.0
N A:CYS136 5.0 12.1 1.0

Arsenic binding site 2 out of 4 in 1pqu

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Arsenic binding site 2 out of 4 in the Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate


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 the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As2375

b:72.5
occ:1.00
AS B:CAC2375 0.0 72.5 1.0
O2 B:CAC2375 1.8 70.3 1.0
O1 B:CAC2375 1.8 70.5 1.0
C2 B:CAC2375 2.0 70.1 1.0
C1 B:CAC2375 2.0 70.7 1.0
NH2 B:ARG103 3.4 18.1 1.0
NH1 B:ARG103 3.7 13.4 1.0
O B:HOH2511 3.9 18.8 1.0
NZ B:LYS246 3.9 19.1 1.0
ND2 B:ASN135 4.0 16.9 1.0
CZ B:ARG103 4.0 16.7 1.0
N B:CYS2374 4.2 29.2 1.0
C6N B:NAP2372 4.4 21.1 1.0
CA B:ASN135 4.4 14.2 1.0
C5N B:NAP2372 4.6 22.6 1.0
CB B:SER100 4.7 16.8 1.0
N B:CYS136 4.7 14.2 1.0
CB B:CYS2374 4.7 29.5 1.0
O2D B:NAP2372 4.7 21.3 1.0
CB B:ASN135 4.9 16.4 1.0
CG B:ASN135 4.9 18.0 1.0
N1N B:NAP2372 4.9 21.6 1.0

Arsenic binding site 3 out of 4 in 1pqu

Go back to Arsenic Binding Sites List in 1pqu
Arsenic binding site 3 out of 4 in the Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate


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 the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As3374

b:74.4
occ:1.00
AS C:CAC3374 0.0 74.4 1.0
O2 C:CAC3374 1.8 73.4 1.0
O1 C:CAC3374 1.8 73.3 1.0
C2 C:CAC3374 2.0 73.6 1.0
C1 C:CAC3374 2.0 74.4 1.0
NH2 C:ARG103 3.4 11.1 1.0
NH1 C:ARG103 3.6 9.4 1.0
ND2 C:ASN135 3.8 14.2 1.0
O C:HOH3536 3.9 21.3 1.0
NZ C:LYS246 3.9 14.6 1.0
CZ C:ARG103 3.9 10.5 1.0
O C:HOH3517 4.0 21.3 1.0
N C:CYS3373 4.2 31.5 1.0
CA C:ASN135 4.3 10.2 1.0
CB C:CYS3373 4.4 32.9 1.0
CB C:SER100 4.7 11.9 1.0
N C:CYS136 4.7 11.9 1.0
CG C:ASN135 4.7 13.8 1.0
CB C:ASN135 4.7 11.2 1.0
CA C:CYS3373 4.8 32.8 1.0
CE C:LYS246 5.0 13.5 1.0

Arsenic binding site 4 out of 4 in 1pqu

Go back to Arsenic Binding Sites List in 1pqu
Arsenic binding site 4 out of 4 in the Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Crystal Structure of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound with Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:As4375

b:64.7
occ:1.00
AS D:CAC4375 0.0 64.7 1.0
O2 D:CAC4375 1.8 63.0 1.0
O1 D:CAC4375 1.8 63.4 1.0
C2 D:CAC4375 2.0 62.7 1.0
C1 D:CAC4375 2.0 62.9 1.0
NZ D:LYS246 3.4 19.6 1.0
NH2 D:ARG103 3.5 15.9 1.0
NH1 D:ARG103 3.6 16.0 1.0
O D:HOH4392 3.9 21.6 1.0
ND2 D:ASN135 3.9 19.8 1.0
CZ D:ARG103 4.0 15.4 1.0
O D:HOH4400 4.3 22.1 1.0
N D:CYS4374 4.3 34.6 1.0
CB D:SER100 4.5 18.3 1.0
CA D:ASN135 4.6 16.4 1.0
CE D:LYS246 4.6 18.2 1.0
CB D:CYS4374 4.8 34.3 1.0
OG D:SER100 4.8 17.1 1.0
O D:HOH4481 4.9 25.9 1.0
CG D:ASN135 4.9 19.8 1.0
CB D:ASN135 4.9 17.4 1.0
O2D D:NAP4372 4.9 26.8 1.0
O D:HOH4485 4.9 25.5 1.0
CD D:LYS246 4.9 15.0 1.0

Reference:

J.Blanco, R.A.Moore, C.R.Faehnle, D.M.Coe, R.E.Viola. The Role of Substrate-Binding Groups in the Mechanism of Aspartate-Beta-Semialdehyde Dehydrogenase. Acta Crystallogr.,Sect.D V. 60 1388 2004.
ISSN: ISSN 0907-4449
PubMed: 15272161
DOI: 10.1107/S0907444904012971
Page generated: Tue Oct 27 16:47:03 2020

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