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Manganese in PDB 7uod: Crystal Structure of A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid

Protein crystallography data

The structure of Crystal Structure of A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid, PDB code: 7uod was solved by J.P.Sousa, E.H.S.Bezerra, M.V.Sales, P.P.Queiroz, F.M.S.Da Silva, C.P.S.Carvalho, V.N.Freire, B.A.M.Rocha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.75 / 1.60
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 68.182, 71.83, 98.809, 90, 90, 90
R / Rfree (%) 19.9 / 22.7

Other elements in 7uod:

The structure of Crystal Structure of A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Chlorine (Cl) 6 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid (pdb code 7uod). 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 A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid, PDB code: 7uod:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 7uod

Go back to Manganese Binding Sites List in 7uod
Manganese binding site 1 out of 2 in the Crystal Structure of A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid


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 A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn303

b:18.2
occ:0.76
O A:HOH419 2.0 17.9 1.0
OE2 A:GLU8 2.0 13.8 1.0
O A:HOH428 2.1 18.8 1.0
OD2 A:ASP10 2.1 18.9 1.0
OD1 A:ASP19 2.1 16.5 1.0
NE2 A:HIS24 2.2 17.7 1.0
CD A:GLU8 3.1 16.9 1.0
CG A:ASP10 3.1 15.4 1.0
CG A:ASP19 3.1 19.2 1.0
CE1 A:HIS24 3.2 15.2 1.0
CD2 A:HIS24 3.2 15.0 1.0
OE1 A:GLU8 3.4 16.0 1.0
CB A:ASP10 3.5 14.3 1.0
OD2 A:ASP19 3.6 18.3 1.0
O A:HOH441 4.0 20.3 1.0
O A:HOH504 4.1 35.6 1.0
OG A:SER34 4.1 19.6 1.0
OD1 A:ASP10 4.2 15.8 1.0
CA A:CA302 4.2 15.3 0.8
ND1 A:HIS24 4.3 19.1 1.0
CB A:ASP19 4.3 18.1 1.0
O A:HOH519 4.3 32.3 1.0
CG A:HIS24 4.4 15.2 1.0
CG A:GLU8 4.4 18.1 1.0
O A:VAL32 4.6 22.2 1.0
CA A:ASP19 4.7 21.1 1.0

Manganese binding site 2 out of 2 in 7uod

Go back to Manganese Binding Sites List in 7uod
Manganese binding site 2 out of 2 in the Crystal Structure of A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid


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 A Lectin From Canavalia Maritima Seed (Conm) Complexed with 2,4-Dichloro-Phenoxyacetic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn303

b:14.4
occ:0.44
NE2 B:HIS24 2.0 24.3 1.0
OD2 B:ASP10 2.1 23.6 1.0
OE2 B:GLU8 2.1 17.6 1.0
O B:HOH424 2.1 25.4 1.0
OD1 B:ASP19 2.1 22.8 1.0
O B:HOH414 2.1 25.4 1.0
CE1 B:HIS24 3.0 18.1 1.0
CG B:ASP10 3.1 28.7 1.0
CG B:ASP19 3.1 27.4 1.0
CD2 B:HIS24 3.1 20.6 1.0
CD B:GLU8 3.1 20.4 1.0
OE1 B:GLU8 3.5 21.0 1.0
CB B:ASP10 3.5 19.5 1.0
OD2 B:ASP19 3.5 25.6 1.0
O B:HOH464 3.9 28.6 1.0
O B:HOH486 4.1 45.5 1.0
ND1 B:HIS24 4.1 20.3 1.0
CA B:CA302 4.1 17.0 0.7
OG B:SER34 4.1 24.5 1.0
OD1 B:ASP10 4.2 24.4 1.0
CG B:HIS24 4.2 18.6 1.0
CB B:ASP19 4.3 26.9 1.0
O B:HOH504 4.3 32.8 1.0
CG B:GLU8 4.5 23.4 1.0
O B:VAL32 4.6 26.4 1.0
CA B:ASP19 4.7 25.9 1.0
CA B:ASP10 5.0 22.2 1.0

Reference:

J.P.Sousa, E.H.S.Bezerra, M.V.Sales, P.P.Queiroz, F.M.S.Da Silva, C.P.S.Carvalho, V.N.Freire, B.A.M.Rocha. Structural Analysis of Canavalia Maritima Lectin Complexed with Auxins To Be Published.
Page generated: Sun Oct 6 10:56:21 2024

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