Manganese in PDB 8fun: Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2

Protein crystallography data

The structure of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2, PDB code: 8fun was solved by M.M.Powell, J.Rittle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.56 / 2.24
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 84.142, 148.923, 234.093, 90, 90, 90
R / Rfree (%) 17.7 / 19.8

Other elements in 8fun:

The structure of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Iron (Fe) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 (pdb code 8fun). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 5 binding sites of Manganese where determined in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2, PDB code: 8fun:
Jump to Manganese binding site number: 1; 2; 3; 4; 5;

Manganese binding site 1 out of 5 in 8fun

Go back to Manganese Binding Sites List in 8fun
Manganese binding site 1 out of 5 in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:24.0
occ:1.00
 OD1 A:ASP340 2.1 21.2 1.0
OE2 A:GLU267 2.2 25.4 1.0
OD2 A:ASP36 2.2 17.1 1.0
NE2 A:HIS38 2.2 17.2 1.0
NE2 A:HIS213 2.3 18.1 1.0
CG A:ASP36 2.9 18.8 1.0
OD1 A:ASP36 3.0 16.2 1.0
CE1 A:HIS38 3.1 24.8 1.0
CE1 A:HIS213 3.1 13.9 1.0
CD A:GLU267 3.1 14.8 1.0
CG A:ASP340 3.2 23.1 1.0
CD2 A:HIS38 3.3 18.2 1.0
CB A:GLU267 3.4 13.5 1.0
CD2 A:HIS213 3.4 15.7 1.0
CG A:GLU267 3.5 16.8 1.0
OD2 A:ASP340 3.7 20.2 1.0
ND1 A:HIS38 4.2 21.4 1.0
ND1 A:HIS343 4.2 18.1 1.0
CE1 A:HIS343 4.2 19.4 1.0
OE1 A:GLU267 4.2 16.1 1.0
O A:HOH519 4.3 15.9 1.0
CB A:ASP340 4.3 17.3 1.0
ND1 A:HIS213 4.3 16.0 1.0
CG A:HIS38 4.3 23.0 1.0
CB A:ASP36 4.4 17.1 1.0
CG A:HIS213 4.5 20.4 1.0
CA A:ASP340 4.6 19.1 1.0
CA A:GLU267 4.8 17.7 1.0
O A:ASP36 5.0 14.8 1.0

Manganese binding site 2 out of 5 in 8fun

Go back to Manganese Binding Sites List in 8fun
Manganese binding site 2 out of 5 in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:36.0
occ:1.00
 ND1 B:HIS340 2.1 29.2 1.0
O B:HOH629 2.1 34.9 1.0
O B:HOH601 2.1 25.2 1.0
OD2 B:ASP337 2.3 25.1 1.0
OE2 B:GLU265 2.4 26.1 1.0
O B:HOH753 2.8 36.0 1.0
CE1 B:HIS340 2.9 27.8 1.0
CG B:HIS340 3.1 30.2 1.0
CG B:ASP337 3.2 25.2 1.0
CD B:GLU265 3.3 24.7 1.0
OE1 B:GLU265 3.4 22.1 1.0
OD1 B:ASP337 3.5 18.3 1.0
CB B:HIS340 3.6 25.8 1.0
FE B:FE504 3.8 33.7 1.0
NE2 B:HIS340 4.1 36.0 1.0
O B:HOH614 4.1 24.6 1.0
OD1 B:ASP342 4.2 24.7 1.0
CD2 B:HIS340 4.2 29.8 1.0
CB B:ASP337 4.6 22.2 1.0
NE2 B:HIS27 4.6 26.6 1.0
CG B:GLU265 4.7 21.8 1.0
CD2 B:HIS27 4.8 28.5 1.0
NE2 B:GLN309 5.0 26.8 1.0

Manganese binding site 3 out of 5 in 8fun

Go back to Manganese Binding Sites List in 8fun
Manganese binding site 3 out of 5 in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn401

b:25.5
occ:1.00
 NE2 C:HIS38 2.1 21.3 1.0
OD1 C:ASP340 2.2 22.3 1.0
OE2 C:GLU267 2.2 15.6 1.0
OD2 C:ASP36 2.2 20.6 1.0
NE2 C:HIS213 2.3 19.7 1.0
CE1 C:HIS38 2.9 22.6 1.0
CG C:ASP36 2.9 25.7 1.0
OD1 C:ASP36 3.0 20.1 1.0
CE1 C:HIS213 3.2 20.1 1.0
CD2 C:HIS38 3.2 18.0 1.0
CD C:GLU267 3.2 18.2 1.0
CG C:ASP340 3.3 22.9 1.0
CD2 C:HIS213 3.4 22.0 1.0
CB C:GLU267 3.4 18.9 1.0
CG C:GLU267 3.6 16.7 1.0
OD2 C:ASP340 3.8 18.6 1.0
ND1 C:HIS38 4.1 21.0 1.0
ND1 C:HIS343 4.1 17.4 1.0
CE1 C:HIS343 4.2 18.3 1.0
O C:HOH506 4.2 22.9 1.0
CG C:HIS38 4.2 16.5 1.0
ND1 C:HIS213 4.3 22.5 1.0
OE1 C:GLU267 4.4 19.2 1.0
CB C:ASP36 4.4 21.3 1.0
CB C:ASP340 4.4 24.6 1.0
CG C:HIS213 4.5 18.2 1.0
CA C:ASP340 4.6 21.7 1.0
CA C:GLU267 4.8 26.4 1.0

Manganese binding site 4 out of 5 in 8fun

Go back to Manganese Binding Sites List in 8fun
Manganese binding site 4 out of 5 in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn401

b:35.1
occ:1.00
 OD2 D:ASP25 2.0 29.6 1.0
NE2 D:HIS27 2.1 32.1 1.0
NE2 D:HIS211 2.1 26.8 1.0
OE1 D:GLU265 2.1 28.5 1.0
OD1 D:ASP337 2.3 29.7 1.0
CG D:ASP25 2.7 26.0 1.0
OD1 D:ASP25 2.7 31.6 1.0
CE1 D:HIS27 2.8 33.4 1.0
CD2 D:HIS211 3.0 23.7 1.0
CE1 D:HIS211 3.1 23.4 1.0
CD2 D:HIS27 3.2 31.4 1.0
CG D:ASP337 3.2 28.5 1.0
CD D:GLU265 3.4 32.0 1.0
OD2 D:ASP337 3.9 27.5 1.0
ND1 D:HIS27 4.0 25.8 1.0
CB D:ASP25 4.1 23.1 1.0
OE2 D:GLU265 4.2 37.4 1.0
CG D:HIS211 4.2 25.6 1.0
MN D:MN402 4.2 46.1 0.8
CB D:ASP337 4.2 30.6 1.0
ND1 D:HIS211 4.2 27.5 1.0
CG D:HIS27 4.2 27.2 1.0
CB D:GLU265 4.3 25.7 1.0
CG D:GLU265 4.4 29.9 1.0
CA D:ASP337 4.6 29.1 1.0
CG1 D:VAL264 4.7 29.2 1.0
ND1 D:HIS340 4.7 51.4 1.0
CE1 D:HIS340 4.7 47.9 1.0

Manganese binding site 5 out of 5 in 8fun

Go back to Manganese Binding Sites List in 8fun
Manganese binding site 5 out of 5 in the Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Enzymatically Active, Mn/Fe Metallated Form of AIBH1H2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn402

b:46.1
occ:0.75
 ND1 D:HIS340 2.1 51.4 1.0
OD2 D:ASP337 2.2 27.5 1.0
O D:HOH593 2.3 47.6 1.0
O D:HOH599 2.3 49.1 1.0
OE2 D:GLU265 2.3 37.4 1.0
CE1 D:HIS340 3.1 47.9 1.0
CD D:GLU265 3.1 32.0 1.0
CG D:HIS340 3.1 53.0 1.0
CG D:ASP337 3.1 28.5 1.0
OE1 D:GLU265 3.2 28.5 1.0
CB D:HIS340 3.4 51.9 1.0
OD1 D:ASP337 3.4 29.7 1.0
OD1 D:ASP342 3.9 57.6 1.0
MN D:MN401 4.2 35.1 1.0
NE2 D:HIS340 4.2 54.4 1.0
CD2 D:HIS340 4.2 47.8 1.0
O D:HOH539 4.3 43.0 1.0
CB D:ASP337 4.5 30.6 1.0
CG D:GLU265 4.5 29.9 1.0
NE2 D:HIS27 4.7 32.1 1.0
OE1 D:GLN309 4.7 49.0 1.0
CD2 D:HIS27 4.8 31.4 1.0
CG D:ASP342 4.9 64.8 1.0
CA D:HIS340 4.9 54.6 1.0
OD2 D:ASP342 5.0 60.1 1.0
NE2 D:GLN309 5.0 45.5 1.0

Reference:

M.M.Powell, G.Rao, R.D.Britt, J.Rittle. Enzymatic Hydroxylation of Aliphatic C-H Bonds By A Mn/Fe Cofactor. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 36945426
DOI: 10.1101/2023.03.10.532131
Page generated: Tue Apr 11 17:18:26 2023

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