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Manganese in PDB 7ney: Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn

Enzymatic activity of Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn

All present enzymatic activity of Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn:
4.1.1.102;

Protein crystallography data

The structure of Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn, PDB code: 7ney was solved by A.Saaret, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.19 / 1.74
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 74.212, 74.212, 346.561, 90, 90, 120
R / Rfree (%) 18.2 / 21.5

Other elements in 7ney:

The structure of Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn also contains other interesting chemical elements:

Potassium (K) 4 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn (pdb code 7ney). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn, PDB code: 7ney:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 7ney

Go back to Manganese Binding Sites List in 7ney
Manganese binding site 1 out of 2 in the Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn604

b:21.4
occ:1.00
O A:HOH824 2.2 18.9 1.0
O2P A:4LU601 2.2 18.5 1.0
ND2 A:ASN178 2.2 15.9 1.0
O A:HOH720 2.3 18.0 1.0
OE2 A:GLU243 2.3 19.3 1.0
ND1 A:HIS201 2.3 20.3 1.0
CE1 A:HIS201 3.2 19.0 1.0
CG A:ASN178 3.2 16.4 1.0
CD A:GLU243 3.3 20.4 1.0
P A:4LU601 3.4 19.0 1.0
CG A:HIS201 3.4 19.2 1.0
OD1 A:ASN178 3.5 19.8 1.0
OE1 A:GLU243 3.6 18.3 1.0
O3P A:4LU601 3.6 20.7 1.0
CB A:HIS201 3.7 19.0 1.0
K A:K602 3.7 34.3 1.0
O1P A:4LU601 4.3 20.1 1.0
CZ2 A:TRP176 4.3 21.5 1.0
CG1 A:ILE237 4.4 24.4 1.0
O A:ILE237 4.4 20.9 1.0
NE2 A:HIS201 4.4 20.7 1.0
CD2 A:HIS201 4.5 20.9 1.0
O5' A:4LU601 4.5 18.8 1.0
CB A:ASN178 4.5 18.5 1.0
O A:VAL241 4.5 21.6 1.0
CG A:GLU243 4.6 21.2 1.0
O A:PRO238 4.7 25.7 1.0
O A:TRP179 4.7 16.6 1.0
NE1 A:TRP176 4.8 21.9 1.0
CE2 A:TRP176 4.9 22.8 1.0

Manganese binding site 2 out of 2 in 7ney

Go back to Manganese Binding Sites List in 7ney
Manganese binding site 2 out of 2 in the Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of T. Atroviride Fdc Wild-Type (Tafdc) in Complex with Prfmn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn604

b:23.2
occ:1.00
O2P B:4LU601 2.2 23.1 1.0
ND2 B:ASN178 2.2 18.9 1.0
OE2 B:GLU243 2.2 21.9 1.0
ND1 B:HIS201 2.2 22.1 1.0
O B:HOH720 2.3 19.6 1.0
O B:HOH707 2.3 19.2 1.0
CE1 B:HIS201 3.1 22.7 1.0
CG B:ASN178 3.2 21.5 1.0
CD B:GLU243 3.2 24.4 1.0
P B:4LU601 3.4 20.1 1.0
CG B:HIS201 3.4 20.6 1.0
OE1 B:GLU243 3.5 20.6 1.0
OD1 B:ASN178 3.5 24.0 1.0
O3P B:4LU601 3.6 21.6 1.0
CB B:HIS201 3.8 18.2 1.0
K B:K603 3.8 37.1 1.0
CG1 B:ILE237 4.3 25.2 1.0
NE2 B:HIS201 4.3 20.6 1.0
O1P B:4LU601 4.3 18.3 1.0
O B:ILE237 4.4 21.0 1.0
CZ2 B:TRP176 4.4 21.4 1.0
O B:VAL241 4.4 24.9 1.0
CD2 B:HIS201 4.4 22.6 1.0
O5' B:4LU601 4.5 21.0 1.0
CB B:ASN178 4.5 19.1 1.0
CG B:GLU243 4.6 25.6 1.0
NE1 B:TRP176 4.6 21.9 1.0
O B:PRO238 4.7 27.6 1.0
O B:TRP179 4.7 20.0 1.0
CE2 B:TRP176 4.9 21.7 1.0
CD1 B:ILE237 5.0 26.2 1.0

Reference:

A.Saaret, B.Villiers, F.Stricher, M.Anissimova, M.Cadillon, R.Spiess, S.Hay, D.Leys. Directed Evolution of Prenylated Fmn-Dependent Fdc Supports Efficient in Vivo Isobutene Production Nat Commun 2021.
ISSN: ESSN 2041-1723
Page generated: Sun Oct 6 10:16:54 2024

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