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Manganese in PDB 1yw9: H-METAP2 Complexed with A849519

Enzymatic activity of H-METAP2 Complexed with A849519

All present enzymatic activity of H-METAP2 Complexed with A849519:
3.4.11.18;

Protein crystallography data

The structure of H-METAP2 Complexed with A849519, PDB code: 1yw9 was solved by C.H.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.68 / 1.64
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.956, 98.801, 100.904, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1yw9:

The structure of H-METAP2 Complexed with A849519 also contains other interesting chemical elements:

Fluorine (F) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the H-METAP2 Complexed with A849519 (pdb code 1yw9). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the H-METAP2 Complexed with A849519, PDB code: 1yw9:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1yw9

Go back to Manganese Binding Sites List in 1yw9
Manganese binding site 1 out of 2 in the H-METAP2 Complexed with A849519


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of H-METAP2 Complexed with A849519 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn480

b:14.6
occ:1.00
OD2 A:ASP262 2.1 15.4 1.0
OE2 A:GLU459 2.1 15.2 1.0
OD2 A:ASP251 2.2 15.1 1.0
O A:HOH516 2.2 16.3 1.0
OD1 A:ASP251 2.2 14.9 1.0
O A:HOH484 2.3 16.6 1.0
CG A:ASP251 2.5 15.1 1.0
CD A:GLU459 3.0 15.4 1.0
CG A:ASP262 3.1 15.5 1.0
OE1 A:GLU459 3.2 15.2 1.0
OD1 A:ASP262 3.3 15.5 1.0
MN A:MN481 3.5 15.6 1.0
CZ A:PHE219 4.0 15.3 1.0
CB A:ASP251 4.0 15.0 1.0
O A:HOH563 4.1 21.5 1.0
NE2 A:GLN457 4.1 15.1 1.0
OE2 A:GLU364 4.2 16.0 1.0
O13 A:A84482 4.2 17.1 1.0
CE2 A:PHE219 4.3 15.3 1.0
O12 A:A84482 4.4 17.2 1.0
CG A:GLU459 4.4 15.4 1.0
CB A:ASP262 4.4 15.5 1.0
CB A:ALA264 4.6 15.4 1.0
C11 A:A84482 4.7 17.4 1.0
N A:CYS263 4.7 15.5 1.0
CD A:GLU364 4.8 16.3 1.0
C A:ASP262 4.8 15.6 1.0
OE1 A:GLU364 4.8 16.3 1.0
CA A:ASP262 4.8 15.7 1.0
CB A:GLU459 4.9 15.4 1.0
CA A:ASP251 4.9 15.0 1.0
CE1 A:PHE219 5.0 15.3 1.0

Manganese binding site 2 out of 2 in 1yw9

Go back to Manganese Binding Sites List in 1yw9
Manganese binding site 2 out of 2 in the H-METAP2 Complexed with A849519


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of H-METAP2 Complexed with A849519 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn481

b:15.6
occ:1.00
OD1 A:ASP262 2.2 15.5 1.0
O12 A:A84482 2.2 17.2 1.0
OE1 A:GLU364 2.2 16.3 1.0
OE1 A:GLU459 2.3 15.2 1.0
NE2 A:HIS331 2.3 17.6 1.0
O A:HOH484 2.3 16.6 1.0
CD A:GLU364 3.1 16.3 1.0
CG A:ASP262 3.1 15.5 1.0
CD2 A:HIS331 3.2 17.8 1.0
CE1 A:HIS331 3.3 17.6 1.0
C11 A:A84482 3.3 17.4 1.0
CD A:GLU459 3.3 15.4 1.0
OE2 A:GLU364 3.4 16.0 1.0
MN A:MN480 3.5 14.6 1.0
OD2 A:ASP262 3.6 15.4 1.0
O13 A:A84482 3.6 17.1 1.0
OE2 A:GLU459 3.7 15.2 1.0
CB A:ALA362 3.9 17.5 1.0
O A:HOH516 4.1 16.3 1.0
CG A:GLU364 4.3 16.4 1.0
C23 A:A84482 4.3 18.6 1.0
CB A:ASP262 4.3 15.5 1.0
CG A:HIS331 4.4 17.8 1.0
ND1 A:HIS331 4.4 17.7 1.0
C10 A:A84482 4.6 17.5 1.0
CG A:GLU459 4.6 15.4 1.0
N14 A:A84482 4.7 18.0 1.0
C22 A:A84482 4.7 18.7 1.0
CD1 A:ILE338 4.9 20.4 1.0

Reference:

G.S.Sheppard, J.Wang, M.Kawai, S.D.Fidanze, N.Y.Bamaung, S.A.Erickson, D.M.Barnes, J.S.Tedrow, L.Kolaczkowski, A.Vasudevan, D.C.Park, G.T.Wang, W.J.Sanders, R.A.Mantei, F.Palazzo, L.Tucker-Garcia, P.Lou, Q.Zhang, C.H.Park, K.H.Kim, A.Petros, E.Olejniczak, D.Nettesheim, P.Hajduk, J.Henkin, R.Lesniewski, S.K.Davidsen, R.L.Bell. Discovery and Optimization of Anthranilic Acid Sulfonamides As Inhibitors of Methionine Aminopeptidase-2: A Structural Basis For the Reduction of Albumin Binding. J.Med.Chem. V. 49 3832 2006.
ISSN: ISSN 0022-2623
PubMed: 16789740
DOI: 10.1021/JM0601001
Page generated: Sat Oct 5 13:15:50 2024

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