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Manganese in PDB 1hqh: Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine

Enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine

All present enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine:
3.5.3.1;

Protein crystallography data

The structure of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine, PDB code: 1hqh was solved by J.D.Cox, E.Cama, D.M.Colleluori, D.E.Ash, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.80
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 88.000, 88.000, 112.400, 90.00, 90.00, 120.00
R / Rfree (%) 28.6 / 25.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine (pdb code 1hqh). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine, PDB code: 1hqh:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 1hqh

Go back to Manganese Binding Sites List in 1hqh
Manganese binding site 1 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine


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 the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:80.7
occ:1.00
 OD2 A:ASP124 2.0 60.8 1.0
OD2 A:ASP128 2.0 83.8 1.0
ND1 A:HIS101 2.2 68.0 1.0
OH1 A:NNH901 2.5 81.9 1.0
OD2 A:ASP232 2.7 64.6 1.0
CG A:ASP128 3.1 83.9 1.0
CG A:ASP124 3.1 61.7 1.0
CG A:HIS101 3.2 68.7 1.0
CE1 A:HIS101 3.2 67.8 1.0
NH1 A:NNH901 3.3 85.2 1.0
CB A:HIS101 3.4 71.1 1.0
OD1 A:ASP128 3.4 84.8 1.0
MN A:MN501 3.4 72.8 1.0
OD1 A:ASP124 3.6 60.7 1.0
CG A:ASP232 3.6 62.9 1.0
CB A:ASP232 3.9 59.6 1.0
NE1 A:TRP122 4.2 67.9 1.0
O A:HIS141 4.3 89.9 1.0
CD2 A:HIS101 4.3 68.2 1.0
NE2 A:HIS101 4.3 68.1 1.0
CB A:ASP124 4.3 61.3 1.0
CB A:ASP128 4.4 83.2 1.0
CZ2 A:TRP122 4.4 69.3 1.0
OD2 A:ASP234 4.5 57.2 1.0
CE2 A:TRP122 4.6 68.7 1.0
CE A:NNH901 4.7 85.2 1.0
OD1 A:ASP232 4.7 62.5 1.0
O A:HIS126 4.7 71.8 1.0
ND1 A:HIS126 4.8 71.0 1.0
CA A:HIS101 4.9 73.5 1.0
CB A:HIS126 4.9 69.5 1.0

Manganese binding site 2 out of 6 in 1hqh

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Manganese binding site 2 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine


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 the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:72.8
occ:1.00
 ND1 A:HIS126 1.7 71.0 1.0
OD2 A:ASP234 1.8 57.2 1.0
OD1 A:ASP124 2.3 60.7 1.0
OD2 A:ASP232 2.4 64.6 1.0
CE1 A:HIS126 2.5 69.8 1.0
OH1 A:NNH901 2.6 81.9 1.0
CG A:ASP234 2.7 56.4 1.0
CG A:HIS126 2.9 69.9 1.0
OD1 A:ASP234 2.9 58.8 1.0
NH1 A:NNH901 3.0 85.2 1.0
CG A:ASP124 3.2 61.7 1.0
OD2 A:ASP124 3.3 60.8 1.0
CG A:ASP232 3.4 62.9 1.0
MN A:MN500 3.4 80.7 1.0
CE A:NNH901 3.5 85.2 1.0
CB A:HIS126 3.5 69.5 1.0
NH2 A:NNH901 3.6 86.2 1.0
N A:HIS126 3.6 68.9 1.0
NE2 A:HIS126 3.7 69.1 1.0
O A:HOH607 3.8 51.4 1.0
CD2 A:HIS126 3.9 69.0 1.0
CB A:ASP234 4.1 52.1 1.0
N A:ALA125 4.1 63.1 1.0
OD1 A:ASP232 4.1 62.5 1.0
CA A:HIS126 4.2 69.8 1.0
CB A:ASP232 4.3 59.6 1.0
CB A:ALA125 4.4 64.2 1.0
OD1 A:ASP128 4.5 84.8 1.0
ND A:NNH901 4.5 84.2 1.0
CB A:ASP124 4.6 61.3 1.0
C A:ALA125 4.6 67.2 1.0
OD2 A:ASP128 4.6 83.8 1.0
CA A:ALA125 4.6 65.5 1.0
O A:HIS126 4.8 71.8 1.0
C A:HIS126 4.9 71.5 1.0
C A:ASP124 5.0 61.6 1.0
CG A:ASP128 5.0 83.9 1.0

Manganese binding site 3 out of 6 in 1hqh

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Manganese binding site 3 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine


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 the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:80.7
occ:1.00
 OD2 B:ASP124 2.0 60.8 1.0
OD2 B:ASP128 2.0 83.8 1.0
ND1 B:HIS101 2.2 68.0 1.0
OH1 B:NNH902 2.5 81.9 1.0
OD2 B:ASP232 2.7 64.6 1.0
CG B:ASP128 3.1 83.9 1.0
CG B:ASP124 3.1 61.7 1.0
CG B:HIS101 3.2 68.7 1.0
CE1 B:HIS101 3.2 67.8 1.0
NH1 B:NNH902 3.3 85.2 1.0
CB B:HIS101 3.4 71.1 1.0
OD1 B:ASP128 3.4 84.8 1.0
MN B:MN503 3.4 72.8 1.0
OD1 B:ASP124 3.6 60.7 1.0
CG B:ASP232 3.6 62.9 1.0
CB B:ASP232 3.9 59.6 1.0
NE1 B:TRP122 4.2 67.9 1.0
O B:HIS141 4.3 89.9 1.0
CD2 B:HIS101 4.3 68.2 1.0
NE2 B:HIS101 4.3 68.1 1.0
CB B:ASP124 4.3 61.3 1.0
CB B:ASP128 4.4 83.2 1.0
CZ2 B:TRP122 4.4 69.3 1.0
OD2 B:ASP234 4.5 57.2 1.0
CE2 B:TRP122 4.6 68.7 1.0
CE B:NNH902 4.7 85.2 1.0
OD1 B:ASP232 4.7 62.5 1.0
O B:HIS126 4.7 71.8 1.0
ND1 B:HIS126 4.8 71.0 1.0
CA B:HIS101 4.9 73.5 1.0
CB B:HIS126 4.9 69.5 1.0

Manganese binding site 4 out of 6 in 1hqh

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Manganese binding site 4 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine


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 the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn503

b:72.8
occ:1.00
 ND1 B:HIS126 1.7 71.0 1.0
OD2 B:ASP234 1.8 57.2 1.0
OD1 B:ASP124 2.3 60.7 1.0
OD2 B:ASP232 2.4 64.6 1.0
CE1 B:HIS126 2.5 69.8 1.0
OH1 B:NNH902 2.6 81.9 1.0
CG B:ASP234 2.7 56.4 1.0
CG B:HIS126 2.9 69.9 1.0
OD1 B:ASP234 2.9 58.8 1.0
NH1 B:NNH902 3.0 85.2 1.0
CG B:ASP124 3.2 61.7 1.0
OD2 B:ASP124 3.3 60.8 1.0
CG B:ASP232 3.4 62.9 1.0
MN B:MN502 3.4 80.7 1.0
CE B:NNH902 3.5 85.2 1.0
CB B:HIS126 3.5 69.5 1.0
NH2 B:NNH902 3.6 86.2 1.0
N B:HIS126 3.6 68.9 1.0
NE2 B:HIS126 3.7 69.1 1.0
O B:HOH614 3.8 51.4 1.0
CD2 B:HIS126 3.9 69.0 1.0
CB B:ASP234 4.1 52.1 1.0
N B:ALA125 4.1 63.1 1.0
OD1 B:ASP232 4.1 62.5 1.0
CA B:HIS126 4.2 69.8 1.0
CB B:ASP232 4.3 59.6 1.0
CB B:ALA125 4.4 64.2 1.0
OD1 B:ASP128 4.5 84.8 1.0
ND B:NNH902 4.5 84.2 1.0
CB B:ASP124 4.6 61.3 1.0
C B:ALA125 4.6 67.2 1.0
OD2 B:ASP128 4.6 83.8 1.0
CA B:ALA125 4.6 65.5 1.0
O B:HIS126 4.8 71.8 1.0
C B:HIS126 4.9 71.5 1.0
C B:ASP124 5.0 61.6 1.0
CG B:ASP128 5.0 83.9 1.0

Manganese binding site 5 out of 6 in 1hqh

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Manganese binding site 5 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn504

b:80.7
occ:1.00
 OD2 C:ASP124 2.0 60.8 1.0
OD2 C:ASP128 2.0 83.8 1.0
ND1 C:HIS101 2.2 68.0 1.0
OH1 C:NNH903 2.5 81.9 1.0
OD2 C:ASP232 2.7 64.6 1.0
CG C:ASP128 3.1 83.9 1.0
CG C:ASP124 3.1 61.7 1.0
CG C:HIS101 3.2 68.7 1.0
CE1 C:HIS101 3.2 67.8 1.0
NH1 C:NNH903 3.3 85.2 1.0
CB C:HIS101 3.4 71.1 1.0
OD1 C:ASP128 3.4 84.8 1.0
MN C:MN505 3.4 72.8 1.0
OD1 C:ASP124 3.6 60.7 1.0
CG C:ASP232 3.6 62.9 1.0
CB C:ASP232 3.9 59.6 1.0
NE1 C:TRP122 4.2 67.9 1.0
O C:HIS141 4.3 89.9 1.0
CD2 C:HIS101 4.3 68.2 1.0
NE2 C:HIS101 4.3 68.1 1.0
CB C:ASP124 4.3 61.3 1.0
CB C:ASP128 4.4 83.2 1.0
CZ2 C:TRP122 4.4 69.3 1.0
OD2 C:ASP234 4.5 57.2 1.0
CE2 C:TRP122 4.6 68.7 1.0
CE C:NNH903 4.7 85.2 1.0
OD1 C:ASP232 4.7 62.5 1.0
O C:HIS126 4.7 71.8 1.0
ND1 C:HIS126 4.8 71.0 1.0
CA C:HIS101 4.9 73.5 1.0
CB C:HIS126 4.9 69.5 1.0

Manganese binding site 6 out of 6 in 1hqh

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Manganese binding site 6 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with Nor-N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn505

b:72.8
occ:1.00
 ND1 C:HIS126 1.7 71.0 1.0
OD2 C:ASP234 1.8 57.2 1.0
OD1 C:ASP124 2.3 60.7 1.0
OD2 C:ASP232 2.4 64.6 1.0
CE1 C:HIS126 2.5 69.8 1.0
OH1 C:NNH903 2.6 81.9 1.0
CG C:ASP234 2.7 56.4 1.0
CG C:HIS126 2.9 69.9 1.0
OD1 C:ASP234 2.9 58.8 1.0
NH1 C:NNH903 3.0 85.2 1.0
CG C:ASP124 3.2 61.7 1.0
OD2 C:ASP124 3.3 60.8 1.0
CG C:ASP232 3.4 62.9 1.0
MN C:MN504 3.4 80.7 1.0
CE C:NNH903 3.5 85.2 1.0
CB C:HIS126 3.5 69.5 1.0
NH2 C:NNH903 3.6 86.2 1.0
N C:HIS126 3.6 68.9 1.0
NE2 C:HIS126 3.7 69.1 1.0
O C:HOH621 3.8 51.4 1.0
CD2 C:HIS126 3.9 69.0 1.0
CB C:ASP234 4.1 52.1 1.0
N C:ALA125 4.1 63.1 1.0
OD1 C:ASP232 4.1 62.5 1.0
CA C:HIS126 4.2 69.8 1.0
CB C:ASP232 4.3 59.6 1.0
CB C:ALA125 4.4 64.2 1.0
OD1 C:ASP128 4.5 84.8 1.0
ND C:NNH903 4.5 84.2 1.0
CB C:ASP124 4.6 61.3 1.0
C C:ALA125 4.6 67.2 1.0
OD2 C:ASP128 4.6 83.8 1.0
CA C:ALA125 4.6 65.5 1.0
O C:HIS126 4.8 71.8 1.0
C C:HIS126 4.9 71.5 1.0
C C:ASP124 5.0 61.6 1.0
CG C:ASP128 5.0 83.9 1.0

Reference:

J.D.Cox, E.Cama, D.M.Colleluori, S.Pethe, J.L.Boucher, D.Mansuy, D.E.Ash, D.W.Christianson. Mechanistic and Metabolic Inferences From the Binding of Substrate Analogues and Products to Arginase. Biochemistry V. 40 2689 2001.
ISSN: ISSN 0006-2960
PubMed: 11258880
DOI: 10.1021/BI002318+
Page generated: Sat Oct 5 10:54:02 2024

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