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Manganese in PDB 1els: Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution

Enzymatic activity of Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution

All present enzymatic activity of Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution:
4.2.1.11;

Protein crystallography data

The structure of Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution, PDB code: 1els was solved by E.Zhang, M.Hatada, J.M.Brewer, L.Lebioda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.40
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 124.100, 124.100, 66.900, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution (pdb code 1els). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution, PDB code: 1els:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1els

Go back to Manganese Binding Sites List in 1els
Manganese binding site 1 out of 2 in the Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn438

b:25.8
occ:1.00
 O A:HOH653 2.1 26.6 1.0
O A:HOH527 2.2 25.0 1.0
O3 A:PAH439 2.2 36.1 1.0
OD2 A:ASP320 2.2 18.7 1.0
OD2 A:ASP246 2.2 20.5 1.0
OE2 A:GLU295 2.2 16.5 1.0
N3 A:PAH439 3.1 41.9 1.0
CG A:ASP246 3.1 18.1 1.0
CD A:GLU295 3.3 14.1 1.0
OD1 A:ASP246 3.3 19.6 1.0
CG A:ASP320 3.3 16.9 1.0
O A:HOH668 3.8 29.6 0.8
O A:HOH751 3.8 46.6 1.0
CB A:ASP320 3.9 16.4 1.0
C2 A:PAH439 3.9 43.0 1.0
OE1 A:GLU295 4.0 14.8 1.0
OD2 A:ASP296 4.2 7.0 1.0
CG A:GLU295 4.3 13.9 1.0
OD1 A:ASP320 4.3 16.8 1.0
NZ A:LYS396 4.3 9.2 1.0
NE2 A:GLN167 4.4 13.2 1.0
CB A:ASP246 4.5 15.8 1.0
OE2 A:GLU168 4.6 22.4 1.0
O2 A:PAH439 4.7 44.7 1.0
C1 A:PAH439 4.8 44.8 1.0
CG A:ASP296 4.8 7.0 1.0
CD2 A:LEU343 4.9 8.6 1.0
CB A:ALA248 4.9 12.2 1.0
OD1 A:ASP321 5.0 14.4 1.0

Manganese binding site 2 out of 2 in 1els

Go back to Manganese Binding Sites List in 1els
Manganese binding site 2 out of 2 in the Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Catalytic Metal Ion Binding in Enolase: the Crystal Structure of Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn440

b:44.6
occ:0.87
 O1P A:PAH439 2.0 45.9 1.0
O3P A:PAH439 2.0 44.7 1.0
O A:GLY37 2.1 47.2 1.0
P A:PAH439 2.1 46.4 1.0
O2P A:PAH439 2.7 46.8 1.0
C A:GLY37 2.8 47.5 1.0
OG A:SER375 3.1 18.8 1.0
CA A:ALA38 3.1 53.0 1.0
N A:ALA38 3.2 49.6 1.0
O A:HOH611 3.4 47.3 0.7
CB A:SER375 3.5 15.3 1.0
N A:SER375 3.6 12.6 1.0
C A:ALA38 3.6 55.4 1.0
N A:SER39 3.8 57.4 1.0
NH2 A:ARG374 3.9 15.0 1.0
CA A:GLY37 3.9 45.1 1.0
C1 A:PAH439 4.0 44.8 1.0
CA A:SER375 4.1 13.1 1.0
NE A:ARG374 4.2 13.4 1.0
O A:HOH730 4.3 29.4 1.0
O A:HOH444 4.4 53.1 1.0
CA A:ARG374 4.5 11.0 1.0
OG A:SER39 4.5 59.8 1.0
O A:ALA38 4.5 55.7 1.0
CZ A:ARG374 4.5 14.7 1.0
C A:ARG374 4.5 11.7 1.0
CB A:ALA38 4.5 52.8 1.0
O A:HOH674 4.5 62.5 1.0
CB A:SER39 4.6 59.5 1.0
CB A:ARG374 4.6 11.3 1.0
O A:HOH768 4.7 71.6 0.9
CA A:SER39 4.8 59.0 1.0
O A:HOH741 4.9 49.9 1.0
N A:GLY37 4.9 41.2 1.0

Reference:

E.Zhang, M.Hatada, J.M.Brewer, L.Lebioda. Catalytic Metal Ion Binding in Enolase: the Crystal Structure of An Enolase-MN2+-Phosphonoacetohydroxamate Complex at 2.4-A Resolution. Biochemistry V. 33 6295 1994.
ISSN: ISSN 0006-2960
PubMed: 8193144
DOI: 10.1021/BI00186A032
Page generated: Tue Dec 15 03:47:22 2020

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