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Manganese in PDB 3mfw: Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate

Enzymatic activity of Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate

All present enzymatic activity of Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate:
3.5.3.1;

Protein crystallography data

The structure of Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate, PDB code: 3mfw was solved by L.Di Costanzo, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.47
Space group P 3
Cell size a, b, c (Å), α, β, γ (°) 90.338, 90.338, 69.429, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 16.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate (pdb code 3mfw). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate, PDB code: 3mfw:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3mfw

Go back to Manganese Binding Sites List in 3mfw
Manganese binding site 1 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn5362

b:20.5
occ:1.00
 OD1 A:ASP124 2.1 12.5 1.0
O4 A:SO4551 2.1 24.9 1.0
OD2 A:ASP232 2.2 19.0 1.0
OD1 A:ASP234 2.2 14.6 1.0
ND1 A:HIS126 2.3 18.1 1.0
OD2 A:ASP234 2.3 16.9 1.0
CG A:ASP234 2.5 17.4 1.0
O1 A:SO4551 2.6 34.1 1.0
S A:SO4551 2.8 34.6 1.0
CG A:ASP124 3.0 16.3 1.0
CG A:ASP232 3.1 18.5 1.0
MN A:MN5363 3.2 19.4 1.0
CE1 A:HIS126 3.2 14.7 1.0
CG A:HIS126 3.4 14.7 1.0
OD2 A:ASP124 3.4 15.2 1.0
OD1 A:ASP232 3.6 17.9 1.0
O3 A:SO4551 3.7 26.7 1.0
CB A:HIS126 3.7 15.1 1.0
CB A:ASP234 4.0 16.4 1.0
N A:HIS126 4.1 12.0 1.0
CB A:ASP232 4.1 16.1 1.0
O2 A:SO4551 4.1 28.1 1.0
NT A:B3U600 4.2 44.7 1.0
N A:ALA125 4.3 12.3 1.0
NE2 A:HIS126 4.3 20.8 1.0
CB A:ASP124 4.4 15.2 1.0
CD2 A:HIS126 4.5 18.2 1.0
OG1 A:THR246 4.5 29.5 1.0
CA A:HIS126 4.5 13.9 1.0
NE2 A:B3U600 4.6 39.8 1.0
OD1 A:ASP128 4.6 16.8 1.0
CE1 A:B3U600 4.7 31.9 1.0
OD2 A:ASP128 4.7 15.8 1.0
O A:HOH436 4.7 18.5 1.0
CA A:ASP124 4.7 13.7 1.0
CB A:ALA125 4.8 16.0 1.0
CA A:ALA125 4.9 11.6 1.0
C A:ALA125 4.9 9.7 1.0
C A:ASP124 4.9 14.0 1.0
CA A:ASP234 4.9 13.1 1.0

Manganese binding site 2 out of 4 in 3mfw

Go back to Manganese Binding Sites List in 3mfw
Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn5363

b:19.4
occ:1.00
 O4 A:SO4551 2.0 24.9 1.0
OD2 A:ASP124 2.1 15.2 1.0
O3 A:SO4551 2.1 26.7 1.0
OD2 A:ASP128 2.1 15.8 1.0
ND1 A:HIS101 2.2 15.9 1.0
OD2 A:ASP232 2.2 19.0 1.0
S A:SO4551 2.4 34.6 1.0
CG A:ASP124 3.0 16.3 1.0
CG A:ASP128 3.1 12.1 1.0
CG A:HIS101 3.1 14.5 1.0
MN A:MN5362 3.2 20.5 1.0
CE1 A:HIS101 3.2 15.1 1.0
CG A:ASP232 3.2 18.5 1.0
CB A:HIS101 3.3 19.4 1.0
OD1 A:ASP124 3.4 12.5 1.0
O1 A:SO4551 3.5 34.1 1.0
OD1 A:ASP128 3.5 16.8 1.0
O2 A:SO4551 3.6 28.1 1.0
CB A:ASP232 3.6 16.1 1.0
CD2 A:HIS101 4.3 15.7 1.0
NE2 A:HIS101 4.3 15.2 1.0
NE1 A:TRP122 4.4 14.2 1.0
OD1 A:ASP232 4.4 17.9 1.0
CB A:ASP124 4.4 15.2 1.0
CB A:ASP128 4.5 17.2 1.0
O A:HIS141 4.5 16.9 1.0
CZ2 A:TRP122 4.6 16.0 1.0
CG A:GLU277 4.7 18.4 1.0
OE2 A:GLU277 4.8 18.8 1.0
CE2 A:TRP122 4.8 13.2 1.0
OD1 A:ASP234 4.9 14.6 1.0
CA A:HIS101 4.9 14.5 1.0
ND1 A:HIS126 4.9 18.1 1.0
OD2 A:ASP234 4.9 16.9 1.0
CB A:HIS126 4.9 15.1 1.0
CA A:ASP232 5.0 14.3 1.0

Manganese binding site 3 out of 4 in 3mfw

Go back to Manganese Binding Sites List in 3mfw
Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn6362

b:25.8
occ:1.00
 OD2 B:ASP232 2.1 23.4 1.0
O4 B:SO4552 2.1 31.2 1.0
OD1 B:ASP234 2.1 20.4 1.0
OD1 B:ASP124 2.2 19.4 1.0
OD2 B:ASP234 2.3 20.1 1.0
ND1 B:HIS126 2.4 26.1 1.0
CG B:ASP234 2.5 27.5 1.0
O1 B:SO4552 2.6 44.7 1.0
S B:SO4552 2.9 41.0 1.0
CG B:ASP232 3.0 27.9 1.0
CG B:ASP124 3.1 19.3 1.0
MN B:MN6363 3.2 27.8 1.0
CE1 B:HIS126 3.3 23.9 1.0
OD2 B:ASP124 3.5 18.0 1.0
CG B:HIS126 3.5 24.7 1.0
OD1 B:ASP232 3.6 20.2 1.0
O3 B:SO4552 3.8 29.1 1.0
CB B:HIS126 3.9 20.3 1.0
CB B:ASP234 4.0 22.7 1.0
CB B:ASP232 4.1 19.9 1.0
NT B:B3U601 4.1 46.6 1.0
O2 B:SO4552 4.1 51.7 1.0
N B:HIS126 4.1 18.6 1.0
N B:ALA125 4.3 16.9 1.0
CB B:ASP124 4.4 19.4 1.0
NE2 B:HIS126 4.4 25.0 1.0
CD2 B:HIS126 4.6 30.1 1.0
NE2 B:B3U601 4.6 38.8 1.0
O B:HOH461 4.6 25.9 1.0
CE1 B:B3U601 4.6 47.0 1.0
CA B:HIS126 4.6 21.2 1.0
OD1 B:ASP128 4.7 20.6 1.0
OD2 B:ASP128 4.7 19.8 1.0
CA B:ASP124 4.8 15.2 1.0
OG1 B:THR246 4.8 38.8 1.0
CA B:ASP234 4.9 16.6 1.0
CB B:ALA125 5.0 18.7 1.0
C B:ALA125 5.0 15.1 1.0
ND1 B:HIS101 5.0 19.5 1.0
C B:ASP124 5.0 21.4 1.0

Manganese binding site 4 out of 4 in 3mfw

Go back to Manganese Binding Sites List in 3mfw
Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Human Arginase I in Complex with L-2- Aminohistidine and Sulphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn6363

b:27.8
occ:1.00
 O4 B:SO4552 2.0 31.2 1.0
ND1 B:HIS101 2.1 19.5 1.0
OD2 B:ASP124 2.1 18.0 1.0
OD2 B:ASP128 2.2 19.8 1.0
O3 B:SO4552 2.3 29.1 1.0
OD2 B:ASP232 2.3 23.4 1.0
S B:SO4552 2.4 41.0 1.0
CG B:ASP124 3.0 19.3 1.0
CG B:HIS101 3.1 19.5 1.0
CE1 B:HIS101 3.1 22.2 1.0
MN B:MN6362 3.2 25.8 1.0
CG B:ASP128 3.2 18.9 1.0
CG B:ASP232 3.3 27.9 1.0
CB B:HIS101 3.3 22.3 1.0
OD1 B:ASP124 3.3 19.4 1.0
O1 B:SO4552 3.5 44.7 1.0
O2 B:SO4552 3.6 51.7 1.0
OD1 B:ASP128 3.6 20.6 1.0
CB B:ASP232 3.6 19.9 1.0
NE2 B:HIS101 4.2 22.1 1.0
CD2 B:HIS101 4.2 30.2 1.0
NE1 B:TRP122 4.4 19.5 1.0
CB B:ASP124 4.4 19.4 1.0
OD1 B:ASP232 4.4 20.2 1.0
CZ2 B:TRP122 4.5 22.0 1.0
CB B:ASP128 4.5 18.6 1.0
O B:HIS141 4.6 27.4 1.0
CG B:GLU277 4.7 23.5 1.0
CE2 B:TRP122 4.7 23.1 1.0
OE2 B:GLU277 4.8 31.0 1.0
CA B:HIS101 4.8 23.3 1.0
OD2 B:ASP234 4.9 20.1 1.0
OD1 B:ASP234 4.9 20.4 1.0
ND1 B:HIS126 5.0 26.1 1.0
CA B:ASP232 5.0 17.6 1.0

Reference:

M.Ilies, L.Di Costanzo, M.L.North, J.A.Scott, D.W.Christianson. 2-Aminoimidazole Amino Acids As Inhibitors of the Binuclear Manganese Metalloenzyme Human Arginase I. J.Med.Chem. V. 53 4266 2010.
ISSN: ISSN 0022-2623
PubMed: 20441173
DOI: 10.1021/JM100306A
Page generated: Sat Oct 5 17:07:35 2024

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