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Manganese in PDB 1r58: Crystal Structure of METAP2 Complexed with A357300

Enzymatic activity of Crystal Structure of METAP2 Complexed with A357300

All present enzymatic activity of Crystal Structure of METAP2 Complexed with A357300:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure of METAP2 Complexed with A357300, PDB code: 1r58 was solved by G.S.Sheppard, J.Wang, M.Kawai, N.Y.Bamaung, R.A.Craig, S.A.Ericken, L.Lynch, J.Patel, F.Yang, X.B.Searle, P.Lou, C.Park, K.H.Kim, J.Henkin, R.Lesniewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 90.179, 99.138, 101.065, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1r58:

The structure of Crystal Structure of METAP2 Complexed with A357300 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of METAP2 Complexed with A357300 (pdb code 1r58). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of METAP2 Complexed with A357300, PDB code: 1r58:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1r58

Go back to Manganese Binding Sites List in 1r58
Manganese binding site 1 out of 2 in the Crystal Structure of METAP2 Complexed with A357300


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 METAP2 Complexed with A357300 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn480

b:14.0
occ:1.00
OD2 A:ASP262 2.1 13.3 1.0
OE2 A:GLU459 2.2 12.8 1.0
OD2 A:ASP251 2.2 12.1 1.0
O10 A:AO5501 2.3 19.8 1.0
OD1 A:ASP251 2.3 13.5 1.0
N8 A:AO5501 2.4 17.7 1.0
CG A:ASP251 2.6 13.6 1.0
CD A:GLU459 3.1 13.6 1.0
CG A:ASP262 3.1 13.8 1.0
C7 A:AO5501 3.1 19.7 1.0
C9 A:AO5501 3.1 20.1 1.0
OE1 A:GLU459 3.2 12.6 1.0
OD1 A:ASP262 3.3 14.3 1.0
MN A:MN481 3.5 14.7 1.0
OE2 A:GLU364 4.0 17.9 1.0
CZ A:PHE219 4.1 14.7 1.0
CB A:ASP251 4.1 13.5 1.0
O A:HOH744 4.1 41.5 1.0
NE2 A:GLN457 4.2 12.6 1.0
CE2 A:PHE219 4.2 14.0 1.0
C6 A:AO5501 4.4 20.1 1.0
C11 A:AO5501 4.4 21.1 1.0
CB A:ASP262 4.4 13.1 1.0
CG A:GLU459 4.4 12.8 1.0
CB A:ALA264 4.6 11.7 1.0
N A:CYS263 4.7 13.2 1.0
CD A:GLU364 4.7 18.1 1.0
OE1 A:GLU364 4.7 16.6 1.0
C A:ASP262 4.7 13.5 1.0
O12 A:AO5501 4.7 19.9 1.0
CA A:ASP262 4.8 13.9 1.0
CA A:ASP251 4.9 13.3 1.0
CB A:GLU459 4.9 12.0 1.0
CE1 A:PHE219 5.0 14.6 1.0
O A:CYS263 5.0 13.0 1.0

Manganese binding site 2 out of 2 in 1r58

Go back to Manganese Binding Sites List in 1r58
Manganese binding site 2 out of 2 in the Crystal Structure of METAP2 Complexed with A357300


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 METAP2 Complexed with A357300 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn481

b:14.7
occ:1.00
OD1 A:ASP262 2.1 14.3 1.0
OE1 A:GLU364 2.1 16.6 1.0
OE1 A:GLU459 2.2 12.6 1.0
NE2 A:HIS331 2.3 16.0 1.0
O10 A:AO5501 2.3 19.8 1.0
O12 A:AO5501 2.5 19.9 1.0
CD A:GLU364 3.0 18.1 1.0
CG A:ASP262 3.1 13.8 1.0
C11 A:AO5501 3.2 21.1 1.0
CD2 A:HIS331 3.2 15.5 1.0
C9 A:AO5501 3.2 20.1 1.0
CD A:GLU459 3.3 13.6 1.0
CE1 A:HIS331 3.3 15.6 1.0
OE2 A:GLU364 3.4 17.9 1.0
MN A:MN480 3.5 14.0 1.0
OD2 A:ASP262 3.6 13.3 1.0
OE2 A:GLU459 3.7 12.8 1.0
C7 A:AO5501 3.8 19.7 1.0
CB A:ALA362 4.0 17.6 1.0
CG A:GLU364 4.3 17.4 1.0
CB A:ASP262 4.3 13.1 1.0
CG A:HIS331 4.4 16.4 1.0
ND1 A:HIS331 4.4 15.6 1.0
O A:HOH660 4.4 37.7 1.0
N8 A:AO5501 4.5 17.7 1.0
CG A:GLU459 4.5 12.8 1.0
CE1 A:HIS339 4.6 23.9 1.0
N13 A:AO5501 4.6 22.4 1.0
CB A:GLU364 4.8 18.1 1.0

Reference:

G.S.Sheppard, J.Wang, M.Kawai, N.Y.Bamaung, R.A.Craig, S.A.Erickson, L.Lynch, J.Patel, F.Yang, X.B.Searle, P.Lou, C.Park, K.H.Kim, J.Henkin, R.Lesniewski. 3-Amino-2-Hydroxyamides and Related Compounds As Inhibitors of Methionine Aminopeptidase-2. Bioorg.Med.Chem.Lett. V. 14 865 2004.
ISSN: ISSN 0960-894X
PubMed: 15012983
DOI: 10.1016/J.BMCL.2003.12.031
Page generated: Tue Dec 15 03:55:00 2020

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