Atomistry » Manganese » PDB 1ho5-1j53 » 1hq5
Atomistry »
  Manganese »
    PDB 1ho5-1j53 »
      1hq5 »

Manganese in PDB 1hq5: Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue

Enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue

All present enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue:
3.5.3.1;

Protein crystallography data

The structure of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue, PDB code: 1hq5 was solved by N.N.Kim, J.D.Cox, R.F.Baggio, F.A.Emig, S.K.Mistry, S.L.Harper, D.W.Speicher, S.M.Morris Jr., D.E.Ash, A.Traish, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.30
Space group P 3
Cell size a, b, c (Å), α, β, γ (°) 91.300, 91.300, 69.400, 90.00, 90.00, 120.00
R / Rfree (%) 15.8 / 19.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue (pdb code 1hq5). 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 the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue, PDB code: 1hq5:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1hq5

Go back to Manganese Binding Sites List in 1hq5
Manganese binding site 1 out of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue


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 S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:28.6
occ:1.00
OD2 A:ASP124 2.1 13.5 1.0
OD2 A:ASP128 2.1 12.2 1.0
OD2 A:ASP232 2.2 17.7 1.0
O3 A:S2C551 2.2 30.2 1.0
ND1 A:HIS101 2.2 23.2 1.0
O1 A:S2C551 2.5 28.3 1.0
B A:S2C551 2.8 30.7 1.0
CG A:HIS101 3.1 23.2 1.0
CG A:ASP128 3.2 13.3 1.0
CG A:ASP124 3.2 13.9 1.0
CB A:HIS101 3.3 22.5 1.0
O2 A:S2C551 3.3 31.6 1.0
CE1 A:HIS101 3.3 22.7 1.0
CG A:ASP232 3.3 17.4 1.0
MN A:MN501 3.4 22.3 1.0
OD1 A:ASP128 3.5 10.9 1.0
OD1 A:ASP124 3.8 12.5 1.0
CB A:ASP232 3.8 18.6 1.0
O A:HIS141 4.1 16.8 1.0
CE A:S2C551 4.2 32.5 1.0
CD2 A:HIS101 4.3 22.2 1.0
NE2 A:HIS101 4.3 20.3 1.0
OD1 A:ASP232 4.4 18.9 1.0
NE1 A:TRP122 4.4 16.1 1.0
CB A:ASP124 4.4 13.9 1.0
CB A:ASP128 4.5 12.7 1.0
CZ2 A:TRP122 4.6 17.6 1.0
CG A:GLU277 4.7 19.7 1.0
CD A:S2C551 4.7 35.3 1.0
CA A:HIS101 4.8 22.8 1.0
CE2 A:TRP122 4.9 16.6 1.0
OE2 A:GLU277 4.9 20.5 1.0

Manganese binding site 2 out of 4 in 1hq5

Go back to Manganese Binding Sites List in 1hq5
Manganese binding site 2 out of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue


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 S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:22.3
occ:1.00
OD1 A:ASP124 2.1 12.5 1.0
O3 A:S2C551 2.2 30.2 1.0
OD2 A:ASP234 2.3 18.6 1.0
OD1 A:ASP234 2.4 16.7 1.0
ND1 A:HIS126 2.5 13.6 1.0
CG A:ASP234 2.7 20.0 1.0
O2 A:S2C551 2.7 31.6 1.0
OD2 A:ASP232 2.7 17.7 1.0
CG A:ASP124 2.9 13.9 1.0
B A:S2C551 3.0 30.7 1.0
OD2 A:ASP124 3.1 13.5 1.0
CG A:ASP232 3.2 17.4 1.0
CE1 A:HIS126 3.3 11.7 1.0
MN A:MN500 3.4 28.6 1.0
CG A:HIS126 3.6 12.1 1.0
OD1 A:ASP232 3.6 18.9 1.0
CE A:S2C551 3.8 32.5 1.0
CB A:HIS126 3.9 12.6 1.0
CB A:ASP232 4.0 18.6 1.0
N A:HIS126 4.1 13.4 1.0
N A:ALA125 4.1 14.8 1.0
O1 A:S2C551 4.1 28.3 1.0
CB A:ASP234 4.2 17.9 1.0
CB A:ASP124 4.3 13.9 1.0
CD A:S2C551 4.3 35.3 1.0
NE2 A:HIS126 4.5 12.7 1.0
CA A:HIS126 4.6 12.2 1.0
CD2 A:HIS126 4.6 12.7 1.0
O A:HOH614 4.7 12.5 1.0
CA A:ASP124 4.7 15.2 1.0
OD1 A:ASP128 4.7 10.9 1.0
CB A:ALA125 4.8 13.2 1.0
C A:ALA125 4.8 13.7 1.0
CA A:ALA125 4.8 13.5 1.0
OD2 A:ASP128 4.8 12.2 1.0
C A:ASP124 4.9 14.9 1.0
O A:THR246 4.9 23.0 1.0
C A:ASP234 5.0 16.2 1.0
O A:ASP234 5.0 16.8 1.0

Manganese binding site 3 out of 4 in 1hq5

Go back to Manganese Binding Sites List in 1hq5
Manganese binding site 3 out of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue


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 S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:27.1
occ:1.00
OD2 B:ASP124 2.1 19.6 1.0
OD2 B:ASP128 2.1 13.7 1.0
OD2 B:ASP232 2.1 21.2 1.0
O3 B:S2C552 2.2 20.0 1.0
ND1 B:HIS101 2.2 11.7 1.0
O1 B:S2C552 2.5 20.1 1.0
B B:S2C552 2.8 19.6 1.0
CG B:HIS101 3.1 11.5 1.0
CG B:ASP128 3.2 14.1 1.0
CB B:HIS101 3.3 12.8 1.0
CG B:ASP124 3.3 15.2 1.0
O2 B:S2C552 3.3 18.7 1.0
CG B:ASP232 3.3 18.9 1.0
CE1 B:HIS101 3.3 13.7 1.0
MN B:MN503 3.4 18.6 1.0
OD1 B:ASP128 3.5 12.3 1.0
OD1 B:ASP124 3.8 10.2 1.0
CB B:ASP232 3.8 18.4 1.0
O B:HIS141 4.1 13.2 1.0
CE B:S2C552 4.2 20.7 1.0
CD2 B:HIS101 4.3 9.6 1.0
OD1 B:ASP232 4.3 19.0 1.0
NE2 B:HIS101 4.3 9.2 1.0
NE1 B:TRP122 4.4 16.2 1.0
CB B:ASP124 4.5 16.3 1.0
CB B:ASP128 4.5 15.7 1.0
CZ2 B:TRP122 4.6 18.1 1.0
CG B:GLU277 4.7 17.5 1.0
CD B:S2C552 4.7 22.7 1.0
CA B:HIS101 4.8 14.3 1.0
CE2 B:TRP122 4.9 16.7 1.0
OE2 B:GLU277 4.9 15.9 1.0

Manganese binding site 4 out of 4 in 1hq5

Go back to Manganese Binding Sites List in 1hq5
Manganese binding site 4 out of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue


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 S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn503

b:18.6
occ:1.00
OD1 B:ASP124 2.1 10.2 1.0
O3 B:S2C552 2.2 20.0 1.0
OD2 B:ASP234 2.3 16.7 1.0
OD1 B:ASP234 2.4 14.6 1.0
ND1 B:HIS126 2.5 15.1 1.0
O2 B:S2C552 2.7 18.7 1.0
CG B:ASP234 2.7 14.3 1.0
OD2 B:ASP232 2.8 21.2 1.0
CG B:ASP124 2.9 15.2 1.0
B B:S2C552 3.0 19.6 1.0
OD2 B:ASP124 3.1 19.6 1.0
CG B:ASP232 3.2 18.9 1.0
CE1 B:HIS126 3.3 13.0 1.0
MN B:MN502 3.4 27.1 1.0
CG B:HIS126 3.6 14.2 1.0
OD1 B:ASP232 3.6 19.0 1.0
CE B:S2C552 3.8 20.7 1.0
CB B:HIS126 4.0 14.1 1.0
CB B:ASP232 4.1 18.4 1.0
N B:ALA125 4.1 13.5 1.0
N B:HIS126 4.1 14.1 1.0
O1 B:S2C552 4.1 20.1 1.0
CB B:ASP234 4.2 13.5 1.0
CB B:ASP124 4.3 16.3 1.0
CD B:S2C552 4.3 22.7 1.0
NE2 B:HIS126 4.5 13.8 1.0
CD2 B:HIS126 4.6 13.4 1.0
CA B:HIS126 4.6 14.0 1.0
CA B:ASP124 4.7 15.8 1.0
OD1 B:ASP128 4.7 12.3 1.0
CB B:ALA125 4.7 11.7 1.0
CA B:ALA125 4.8 13.1 1.0
C B:ALA125 4.8 13.6 1.0
OD2 B:ASP128 4.8 13.7 1.0
C B:ASP124 4.9 15.4 1.0
O B:THR246 4.9 19.4 1.0
C B:ASP234 5.0 14.7 1.0
O B:ASP234 5.0 17.0 1.0

Reference:

N.N.Kim, J.D.Cox, R.F.Baggio, F.A.Emig, S.K.Mistry, S.L.Harper, D.W.Speicher, S.M.Morris Jr., D.E.Ash, A.Traish, D.W.Christianson. Probing Erectile Function: S-(2-Boronoethyl)-L-Cysteine Binds to Arginase As A Transition State Analogue and Enhances Smooth Muscle Relaxation in Human Penile Corpus Cavernosum. Biochemistry V. 40 2678 2001.
ISSN: ISSN 0006-2960
PubMed: 11258879
DOI: 10.1021/BI002317H
Page generated: Sat Oct 5 10:54:01 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy