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Manganese in PDB 1t4s: Arginase-L-Valine Complex

Enzymatic activity of Arginase-L-Valine Complex

All present enzymatic activity of Arginase-L-Valine Complex:
3.5.3.1;

Protein crystallography data

The structure of Arginase-L-Valine Complex, PDB code: 1t4s was solved by E.Cama, S.Pethe, J.-L.Boucher, H.Shoufa, F.A.Emig, D.E.Ash, R.E.Viola, D.Mansuy, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.74 / 2.80
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 87.800, 87.800, 110.500, 90.00, 90.00, 120.00
R / Rfree (%) 25.8 / 29.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Arginase-L-Valine Complex (pdb code 1t4s). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the Arginase-L-Valine Complex, PDB code: 1t4s:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 1t4s

Go back to Manganese Binding Sites List in 1t4s
Manganese binding site 1 out of 6 in the Arginase-L-Valine Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Arginase-L-Valine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:79.0
occ:1.00
ND1 A:HIS126 2.1 82.1 1.0
OD2 A:ASP234 2.3 68.3 1.0
OD2 A:ASP232 2.3 56.2 1.0
OD1 A:ASP124 2.3 73.3 1.0
OD1 A:ASP234 2.5 69.1 1.0
O A:HOH729 2.7 97.0 1.0
CG A:ASP234 2.7 68.3 1.0
CE1 A:HIS126 2.8 80.5 1.0
OD2 A:ASP124 2.8 76.8 1.0
CG A:ASP124 2.8 74.8 1.0
CG A:ASP232 3.1 58.3 1.0
MN A:MN501 3.1 86.4 1.0
CG A:HIS126 3.3 81.9 1.0
OD1 A:ASP232 3.7 56.2 1.0
CB A:HIS126 3.9 81.8 1.0
N A:HIS126 4.0 77.8 1.0
N A:ALA125 4.0 80.5 1.0
CB A:ASP232 4.0 58.4 1.0
NE2 A:HIS126 4.1 79.5 1.0
CB A:ASP234 4.2 66.0 1.0
OD1 A:ASP128 4.2 94.5 1.0
CB A:ASP124 4.2 74.6 1.0
CD2 A:HIS126 4.3 81.0 1.0
OD2 A:ASP128 4.4 95.8 1.0
CA A:HIS126 4.5 80.5 1.0
OG1 A:THR246 4.6 72.7 1.0
CA A:ASP124 4.7 75.8 1.0
C A:ALA125 4.8 80.4 1.0
CB A:ALA125 4.8 76.3 1.0
CA A:ALA125 4.8 80.6 1.0
CG A:ASP128 4.8 93.8 1.0
C A:ASP124 4.8 77.5 1.0
ND1 A:HIS101 5.0 83.8 1.0

Manganese binding site 2 out of 6 in 1t4s

Go back to Manganese Binding Sites List in 1t4s
Manganese binding site 2 out of 6 in the Arginase-L-Valine Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Arginase-L-Valine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:86.4
occ:1.00
OD2 A:ASP124 2.1 76.8 1.0
OD2 A:ASP128 2.1 95.8 1.0
ND1 A:HIS101 2.3 83.8 1.0
OD2 A:ASP232 2.3 56.2 1.0
O A:HOH729 2.4 97.0 1.0
CG A:ASP128 3.0 93.8 1.0
MN A:MN500 3.1 79.0 1.0
CG A:HIS101 3.2 83.5 1.0
OD1 A:ASP128 3.3 94.5 1.0
CG A:ASP124 3.3 74.8 1.0
CE1 A:HIS101 3.3 85.0 1.0
CB A:HIS101 3.3 81.9 1.0
CG A:ASP232 3.4 58.3 1.0
CB A:ASP232 3.8 58.4 1.0
OD1 A:ASP124 3.9 73.3 1.0
O A:HIS141 4.3 91.1 1.0
CB A:ASP128 4.3 91.7 1.0
CD2 A:HIS101 4.3 83.7 1.0
NE2 A:HIS101 4.4 85.7 1.0
CB A:ASP124 4.4 74.6 1.0
OD1 A:ASP232 4.5 56.2 1.0
NE1 A:TRP122 4.5 78.6 1.0
OE2 A:GLU277 4.6 74.0 1.0
CZ2 A:TRP122 4.7 79.4 1.0
ND1 A:HIS126 4.7 82.1 1.0
OD2 A:ASP234 4.7 68.3 1.0
CG A:GLU277 4.8 74.8 1.0
CA A:HIS101 4.9 76.2 1.0
CE2 A:TRP122 5.0 78.7 1.0
OD1 A:ASP234 5.0 69.1 1.0

Manganese binding site 3 out of 6 in 1t4s

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Manganese binding site 3 out of 6 in the Arginase-L-Valine Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Arginase-L-Valine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:72.5
occ:1.00
ND1 B:HIS126 2.1 73.3 1.0
OD2 B:ASP232 2.1 63.3 1.0
OD1 B:ASP124 2.2 72.3 1.0
OD2 B:ASP234 2.2 71.0 1.0
OD1 B:ASP234 2.5 73.1 1.0
CG B:ASP234 2.7 70.8 1.0
O B:HOH730 2.7 84.2 1.0
CE1 B:HIS126 2.8 74.4 1.0
CG B:ASP124 2.8 71.3 1.0
OD2 B:ASP124 2.9 70.6 1.0
CG B:ASP232 3.0 64.3 1.0
MN B:MN503 3.1 73.8 1.0
CG B:HIS126 3.3 74.3 1.0
OD1 B:ASP232 3.6 63.2 1.0
CB B:HIS126 3.9 74.9 1.0
CB B:ASP232 4.0 63.0 1.0
NE2 B:HIS126 4.0 73.9 1.0
N B:HIS126 4.0 76.8 1.0
N B:ALA125 4.1 75.2 1.0
CB B:ASP234 4.2 67.8 1.0
CB B:ASP124 4.2 70.1 1.0
CD2 B:HIS126 4.3 74.2 1.0
OD1 B:ASP128 4.3 93.1 1.0
OD2 B:ASP128 4.5 93.9 1.0
O B:HOH726 4.5 56.3 1.0
OG1 B:THR246 4.5 66.5 1.0
CA B:HIS126 4.6 78.2 1.0
CA B:ASP124 4.7 69.2 1.0
CB B:ALA125 4.8 73.6 1.0
CG B:ASP128 4.8 92.2 1.0
CA B:ALA125 4.8 75.6 1.0
C B:ALA125 4.9 76.3 1.0
C B:ASP124 4.9 70.8 1.0

Manganese binding site 4 out of 6 in 1t4s

Go back to Manganese Binding Sites List in 1t4s
Manganese binding site 4 out of 6 in the Arginase-L-Valine Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Arginase-L-Valine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn503

b:73.8
occ:1.00
OD2 B:ASP124 2.1 70.6 1.0
OD2 B:ASP128 2.2 93.9 1.0
ND1 B:HIS101 2.3 70.0 1.0
OD2 B:ASP232 2.3 63.3 1.0
O B:HOH730 2.4 84.2 1.0
CG B:ASP128 3.1 92.2 1.0
MN B:MN502 3.1 72.5 1.0
CG B:HIS101 3.2 69.0 1.0
CG B:ASP124 3.3 71.3 1.0
CB B:HIS101 3.3 69.0 1.0
OD1 B:ASP128 3.3 93.1 1.0
CG B:ASP232 3.4 64.3 1.0
CE1 B:HIS101 3.4 68.7 1.0
CB B:ASP232 3.8 63.0 1.0
OD1 B:ASP124 3.8 72.3 1.0
O B:HIS141 4.3 91.5 1.0
CB B:ASP128 4.4 89.8 1.0
CD2 B:HIS101 4.4 67.2 1.0
CB B:ASP124 4.4 70.1 1.0
NE2 B:HIS101 4.4 67.2 1.0
OD1 B:ASP232 4.4 63.2 1.0
NE1 B:TRP122 4.6 84.1 1.0
OE2 B:GLU277 4.6 71.7 1.0
ND1 B:HIS126 4.7 73.3 1.0
CZ2 B:TRP122 4.7 85.5 1.0
OD2 B:ASP234 4.7 71.0 1.0
CG B:GLU277 4.7 71.0 1.0
CA B:HIS101 4.8 75.2 1.0
CE2 B:TRP122 5.0 84.2 1.0

Manganese binding site 5 out of 6 in 1t4s

Go back to Manganese Binding Sites List in 1t4s
Manganese binding site 5 out of 6 in the Arginase-L-Valine Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Arginase-L-Valine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn504

b:58.1
occ:1.00
ND1 C:HIS126 2.1 71.7 1.0
OD2 C:ASP234 2.2 65.6 1.0
OD2 C:ASP232 2.2 48.7 1.0
OD1 C:ASP124 2.3 72.2 1.0
OD1 C:ASP234 2.5 61.5 1.0
CG C:ASP234 2.7 63.2 1.0
O C:HOH728 2.8 37.7 1.0
CE1 C:HIS126 2.8 73.0 1.0
CG C:ASP124 2.9 71.5 1.0
OD2 C:ASP124 2.9 73.4 1.0
CG C:ASP232 3.0 50.7 1.0
MN C:MN505 3.1 81.4 1.0
CG C:HIS126 3.4 73.2 1.0
OD1 C:ASP232 3.6 49.4 1.0
CB C:HIS126 3.9 73.8 1.0
N C:HIS126 4.0 74.2 1.0
CB C:ASP232 4.0 52.1 1.0
NE2 C:HIS126 4.0 72.6 1.0
N C:ALA125 4.0 73.2 1.0
CB C:ASP234 4.2 59.7 1.0
CB C:ASP124 4.2 70.2 1.0
OD1 C:ASP128 4.3 86.6 1.0
CD2 C:HIS126 4.3 72.0 1.0
OG1 C:THR246 4.5 64.8 1.0
OD2 C:ASP128 4.5 86.4 1.0
CA C:HIS126 4.6 75.3 1.0
CA C:ASP124 4.7 61.7 1.0
CB C:ALA125 4.8 74.8 1.0
CA C:ALA125 4.8 74.2 1.0
C C:ALA125 4.8 75.2 1.0
C C:ASP124 4.8 64.0 1.0
CG C:ASP128 4.9 85.3 1.0

Manganese binding site 6 out of 6 in 1t4s

Go back to Manganese Binding Sites List in 1t4s
Manganese binding site 6 out of 6 in the Arginase-L-Valine Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Arginase-L-Valine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn505

b:81.4
occ:1.00
OD2 C:ASP124 2.1 73.4 1.0
OD2 C:ASP128 2.2 86.4 1.0
OD2 C:ASP232 2.3 48.7 1.0
O C:HOH728 2.3 37.7 1.0
ND1 C:HIS101 2.3 65.8 1.0
CG C:ASP128 3.1 85.3 1.0
MN C:MN504 3.1 58.1 1.0
CG C:HIS101 3.2 67.1 1.0
CG C:ASP124 3.3 71.5 1.0
OD1 C:ASP128 3.3 86.6 1.0
CB C:HIS101 3.3 68.2 1.0
CG C:ASP232 3.3 50.7 1.0
CE1 C:HIS101 3.4 67.4 1.0
CB C:ASP232 3.8 52.1 1.0
OD1 C:ASP124 3.8 72.2 1.0
O C:HIS141 4.3 92.0 1.0
CD2 C:HIS101 4.4 65.7 1.0
CB C:ASP124 4.4 70.2 1.0
CB C:ASP128 4.4 84.6 1.0
NE2 C:HIS101 4.4 64.9 1.0
OD1 C:ASP232 4.4 49.4 1.0
NE1 C:TRP122 4.6 64.3 1.0
ND1 C:HIS126 4.7 71.7 1.0
CZ2 C:TRP122 4.7 69.1 1.0
OE2 C:GLU277 4.7 69.8 1.0
CG C:GLU277 4.8 68.9 1.0
OD2 C:ASP234 4.8 65.6 1.0
CA C:HIS101 4.9 74.7 1.0
OD1 C:ASP234 5.0 61.5 1.0
CE2 C:TRP122 5.0 67.8 1.0

Reference:

E.Cama, S.Pethe, J.-L.Boucher, S.Han, F.A.Emig, D.E.Ash, R.E.Viola, D.Mansuy, D.W.Christianson. Inhibitor Coordination Interactions in the Binuclear Manganese Cluster of Arginase Biochemistry V. 43 8987 2004.
ISSN: ISSN 0006-2960
PubMed: 15248756
DOI: 10.1021/BI0491705
Page generated: Sat Oct 5 12:28:58 2024

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