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Manganese in PDB 4ruh: Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A

Enzymatic activity of Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A

All present enzymatic activity of Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A:
3.4.13.18;

Protein crystallography data

The structure of Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A, PDB code: 4ruh was solved by V.Pandya, A.Kaushik, A.K.Singh, R.P.Singh, S.Kumaran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.60 / 2.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 87.090, 100.070, 105.830, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 28.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A (pdb code 4ruh). 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 Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A, PDB code: 4ruh:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 4ruh

Go back to Manganese Binding Sites List in 4ruh
Manganese binding site 1 out of 4 in the Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A


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 Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:6.5
occ:1.00
 O2 A:BES501 1.8 10.5 1.0
OD2 A:ASP132 2.1 10.1 1.0
N2 A:BES501 2.2 6.1 1.0
OD1 A:ASP195 2.2 10.2 1.0
OD2 A:ASP195 2.3 9.9 1.0
NE2 A:HIS99 2.4 10.3 1.0
CG A:ASP195 2.6 10.8 1.0
C2 A:BES501 2.9 9.1 1.0
CG A:ASP132 3.0 7.2 1.0
C1 A:BES501 3.1 6.7 1.0
CE1 A:HIS99 3.2 12.7 1.0
OD1 A:ASP132 3.4 6.4 1.0
MN A:MN503 3.5 5.5 1.0
CD2 A:HIS99 3.5 7.2 1.0
OE2 A:GLU167 3.7 13.8 1.0
O A:HOH723 3.9 6.8 1.0
CB A:ASP133 4.0 6.3 1.0
OE1 A:GLU166 4.1 6.1 1.0
CB A:ASP195 4.1 7.3 1.0
C3 A:BES501 4.1 8.3 1.0
CB A:ASP132 4.2 9.7 1.0
O3 A:BES501 4.3 7.8 1.0
C6 A:BES501 4.4 9.8 1.0
O A:ASP195 4.4 8.4 1.0
ND1 A:HIS99 4.4 9.2 1.0
CA A:ASP132 4.4 9.6 1.0
CG A:ASP133 4.5 10.1 1.0
CD A:GLU167 4.5 8.5 1.0
OH A:TYR197 4.5 10.3 1.0
CD A:GLU166 4.6 7.8 1.0
CG A:HIS99 4.6 7.8 1.0
C A:ASP132 4.7 9.4 1.0
CA A:ASP195 4.8 9.2 1.0
OE2 A:GLU166 4.8 10.4 1.0
CA A:ASP133 4.9 8.1 1.0
OD1 A:ASP133 4.9 6.9 1.0
C A:ASP195 4.9 10.2 1.0
OE1 A:GLU167 4.9 7.1 1.0

Manganese binding site 2 out of 4 in 4ruh

Go back to Manganese Binding Sites List in 4ruh
Manganese binding site 2 out of 4 in the Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A


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 Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn503

b:5.5
occ:1.00
 O3 A:BES501 2.0 7.8 1.0
OE2 A:GLU167 2.2 13.8 1.0
CE1 A:HIS445 2.2 8.0 1.0
OD1 A:ASP132 2.3 6.4 1.0
OE1 A:GLU167 2.3 7.1 1.0
CD A:GLU167 2.6 8.5 1.0
O2 A:BES501 2.6 10.5 1.0
NE2 A:HIS445 2.6 8.9 1.0
C3 A:BES501 2.8 8.3 1.0
CG A:ASP132 3.0 7.2 1.0
C2 A:BES501 3.1 9.1 1.0
OD2 A:ASP132 3.1 10.1 1.0
ND1 A:HIS445 3.5 9.2 1.0
MN A:MN502 3.5 6.5 1.0
C1 A:BES501 3.6 6.7 1.0
CD2 A:HIS445 3.9 9.3 1.0
N2 A:BES501 4.0 6.1 1.0
O A:HOH614 4.0 6.5 1.0
N1 A:BES501 4.0 9.0 1.0
CG A:GLU167 4.1 6.0 1.0
OE1 A:GLU166 4.2 6.1 1.0
NE2 A:GLN103 4.3 9.0 1.0
CG A:GLN103 4.3 7.3 1.0
CG A:HIS445 4.3 10.5 1.0
CB A:ASP132 4.4 9.7 1.0
CE1 A:HIS99 4.6 12.7 1.0
C4 A:BES501 4.7 10.8 1.0
NE2 B:HIS228 4.7 14.3 1.0
NE2 A:HIS99 4.7 10.3 1.0
CD A:GLN103 4.7 12.9 1.0
CD2 B:HIS228 4.9 7.7 1.0
O A:HOH687 5.0 10.1 1.0

Manganese binding site 3 out of 4 in 4ruh

Go back to Manganese Binding Sites List in 4ruh
Manganese binding site 3 out of 4 in the Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A


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 Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:7.3
occ:1.00
 OD2 B:ASP132 2.1 8.4 1.0
O2 B:BES501 2.1 5.0 1.0
OD1 B:ASP195 2.1 7.6 1.0
OD2 B:ASP195 2.2 8.1 1.0
N2 B:BES501 2.2 7.1 1.0
NE2 B:HIS99 2.3 11.1 1.0
CG B:ASP195 2.5 8.3 1.0
C2 B:BES501 3.0 7.2 1.0
CG B:ASP132 3.1 10.1 1.0
C1 B:BES501 3.1 4.7 1.0
CD2 B:HIS99 3.2 9.3 1.0
CE1 B:HIS99 3.4 12.7 1.0
OD1 B:ASP132 3.5 4.6 1.0
OE1 B:GLU166 3.6 8.4 1.0
MN B:MN503 3.6 8.2 1.0
CB B:ASP195 4.0 10.3 1.0
CB B:ASP133 4.1 13.1 1.0
OE2 B:GLU167 4.1 5.4 1.0
OH B:TYR197 4.2 8.0 1.0
C6 B:BES501 4.2 6.6 1.0
O B:ASP195 4.2 12.8 1.0
CD B:GLU166 4.2 8.6 1.0
O B:HOH648 4.3 8.1 1.0
C3 B:BES501 4.3 8.5 1.0
CB B:ASP132 4.4 10.8 1.0
CG B:HIS99 4.4 10.2 1.0
ND1 B:HIS99 4.4 9.6 1.0
OE2 B:GLU166 4.5 9.5 1.0
CG B:ASP133 4.5 13.2 1.0
CD B:GLU167 4.6 8.8 1.0
CA B:ASP132 4.6 9.8 1.0
CA B:ASP195 4.8 8.6 1.0
C B:ASP195 4.8 11.0 1.0
O3 B:BES501 4.8 6.8 1.0
C B:ASP132 4.9 12.8 1.0
OD1 B:ASP133 4.9 8.2 1.0
OE1 B:GLU167 4.9 7.4 1.0
OD2 B:ASP133 5.0 13.0 1.0
CA B:ASP133 5.0 10.1 1.0

Manganese binding site 4 out of 4 in 4ruh

Go back to Manganese Binding Sites List in 4ruh
Manganese binding site 4 out of 4 in the Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A


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 Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn503

b:8.2
occ:1.00
 NE2 B:HIS445 1.9 18.3 1.0
OE2 B:GLU167 2.1 5.4 1.0
OD1 B:ASP132 2.2 4.6 1.0
O2 B:BES501 2.2 5.0 1.0
O3 B:BES501 2.3 6.8 1.0
OE1 B:GLU167 2.3 7.4 1.0
CE1 B:HIS445 2.4 6.9 1.0
CD B:GLU167 2.5 8.8 1.0
C3 B:BES501 2.7 8.5 1.0
C2 B:BES501 2.8 7.2 1.0
CD2 B:HIS445 3.2 9.3 1.0
CG B:ASP132 3.2 10.1 1.0
C1 B:BES501 3.4 4.7 1.0
OD2 B:ASP132 3.5 8.4 1.0
ND1 B:HIS445 3.6 6.5 1.0
MN B:MN502 3.6 7.3 1.0
N2 B:BES501 3.8 7.1 1.0
O B:HOH602 4.0 4.3 1.0
CG B:HIS445 4.0 10.5 1.0
N1 B:BES501 4.0 11.7 1.0
CG B:GLU167 4.1 6.8 1.0
OE1 B:GLU166 4.2 8.4 1.0
NE2 A:HIS228 4.3 6.0 1.0
NE2 B:GLN103 4.4 3.0 1.0
CG B:GLN103 4.4 5.8 1.0
NE2 B:HIS99 4.6 11.1 1.0
CB B:ASP132 4.6 10.8 1.0
CD2 A:HIS228 4.6 4.8 1.0
CD B:GLN103 4.7 4.5 1.0
CE1 B:HIS99 4.7 12.7 1.0
C4 B:BES501 4.8 9.6 1.0
OH B:TYR197 4.8 8.0 1.0
C6 B:BES501 4.8 6.6 1.0

Reference:

V.Pandya, A.Kaushik, A.K.Singh, R.P.Singh, S.Kumaran. Crystal Structure of Human Carnosinase-2 (CN2) in Complex with Inhibitor, Bestatin at 2.25 A To Be Published.
Page generated: Sat Oct 5 21:12:01 2024

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