Atomistry » Manganese » PDB 2dvd-2fer » 2ea2
Atomistry »
  Manganese »
    PDB 2dvd-2fer »
      2ea2 »

Manganese in PDB 2ea2: H-METAP2 Complexed with A773812

Enzymatic activity of H-METAP2 Complexed with A773812

All present enzymatic activity of H-METAP2 Complexed with A773812:
3.4.11.18;

Protein crystallography data

The structure of H-METAP2 Complexed with A773812, PDB code: 2ea2 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) 16.91 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.721, 99.060, 100.855, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 2ea2:

The structure of H-METAP2 Complexed with A773812 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 A773812 (pdb code 2ea2). 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 A773812, PDB code: 2ea2:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2ea2

Go back to Manganese Binding Sites List in 2ea2
Manganese binding site 1 out of 2 in the H-METAP2 Complexed with A773812


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 A773812 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn480

b:22.2
occ:1.00
OE2 A:GLU459 2.2 19.3 1.0
OD2 A:ASP251 2.2 16.5 1.0
OD2 A:ASP262 2.2 16.7 1.0
OD1 A:ASP251 2.5 16.6 1.0
O A:HOH613 2.7 6.0 0.5
CG A:ASP251 2.7 16.4 1.0
CG A:ASP262 3.1 16.5 1.0
CD A:GLU459 3.1 19.1 1.0
OD1 A:ASP262 3.2 16.4 1.0
MN A:MN481 3.3 20.2 1.0
OE1 A:GLU459 3.4 19.0 1.0
OE2 A:GLU364 3.8 19.3 1.0
CB A:ASP251 4.2 16.1 1.0
CZ A:PHE219 4.2 18.0 1.0
O12 A:F77482 4.2 25.7 1.0
NE2 A:GLN457 4.2 18.7 1.0
O A:HOH610 4.3 9.7 1.0
O11 A:F77482 4.4 25.9 1.0
CB A:ASP262 4.5 16.6 1.0
CG A:GLU459 4.5 19.2 1.0
CE2 A:PHE219 4.5 18.1 1.0
CD A:GLU364 4.6 19.2 1.0
CB A:ALA264 4.6 16.0 1.0
C10 A:F77482 4.6 25.9 1.0
N A:CYS263 4.8 16.7 1.0
OE1 A:GLU364 4.8 19.3 1.0
C A:ASP262 4.8 16.9 1.0
CB A:GLU459 4.9 19.0 1.0
CA A:ASP262 4.9 16.8 1.0
CE1 A:PHE219 5.0 18.4 1.0

Manganese binding site 2 out of 2 in 2ea2

Go back to Manganese Binding Sites List in 2ea2
Manganese binding site 2 out of 2 in the H-METAP2 Complexed with A773812


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 A773812 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn481

b:20.2
occ:1.00
OD1 A:ASP262 2.2 16.4 1.0
OE1 A:GLU459 2.2 19.0 1.0
O11 A:F77482 2.4 25.9 1.0
OE1 A:GLU364 2.4 19.3 1.0
NE2 A:HIS331 2.5 19.5 1.0
CD A:GLU364 3.1 19.2 1.0
CD A:GLU459 3.2 19.1 1.0
CG A:ASP262 3.2 16.5 1.0
OE2 A:GLU364 3.3 19.3 1.0
MN A:MN480 3.3 22.2 1.0
C10 A:F77482 3.3 25.9 1.0
CD2 A:HIS331 3.3 19.6 1.0
O12 A:F77482 3.5 25.7 1.0
OE2 A:GLU459 3.5 19.3 1.0
CE1 A:HIS331 3.5 19.6 1.0
OD2 A:ASP262 3.7 16.7 1.0
CB A:ALA362 4.1 19.8 1.0
CG A:GLU364 4.3 19.0 1.0
C18 A:F77482 4.3 27.1 1.0
O A:HOH613 4.4 6.0 0.5
CB A:ASP262 4.4 16.6 1.0
CG A:GLU459 4.5 19.2 1.0
CG A:HIS331 4.5 19.7 1.0
ND1 A:HIS331 4.6 19.5 1.0
C7 A:F77482 4.7 26.0 1.0
C19 A:F77482 4.7 27.1 1.0
N13 A:F77482 4.9 26.9 1.0
CD1 A:ILE338 4.9 26.7 1.0

Reference:

G.T.Wang, R.A.Mantei, M.Kawai, J.S.Tedrow, D.M.Barnes, J.Wang, Q.Zhang, P.Lou, L.A.Garcia, J.Bouska, M.Yates, C.Park, R.A.Judge, R.Lesniewski, G.S.Sheppard, R.L.Bell. Lead Optimization of Methionine Aminopeptidase-2 (METAP2) Inhibitors Containing Sulfonamides of 5,6-Disubstituted Anthranilic Acids Bioorg.Med.Chem.Lett. V. 17 2817 2007.
ISSN: ISSN 0960-894X
PubMed: 17350258
DOI: 10.1016/J.BMCL.2007.02.062
Page generated: Tue Dec 15 04:01:17 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy