Atomistry » Iron » PDB 3s6b-3sxt » 3sjl
Atomistry »
  Iron »
    PDB 3s6b-3sxt »
      3sjl »

Iron in PDB 3sjl: Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3sjl was solved by L.M.R.Jensen, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.39 / 1.63
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 55.606, 89.001, 104.812, 67.05, 79.51, 79.72
R / Rfree (%) 14.2 / 18

Other elements in 3sjl:

The structure of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Sodium (Na) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 3sjl). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3sjl:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3sjl

Go back to Iron Binding Sites List in 3sjl
Iron binding site 1 out of 4 in the Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:15.6
occ:1.00
FE A:HEC500 0.0 15.6 1.0
NC A:HEC500 2.0 13.7 1.0
NB A:HEC500 2.0 15.1 1.0
ND A:HEC500 2.0 14.7 1.0
NA A:HEC500 2.0 14.6 1.0
OE2 A:GLU113 2.1 16.2 1.0
NE2 A:HIS35 2.1 17.7 1.0
C4B A:HEC500 3.0 16.5 1.0
C4D A:HEC500 3.0 13.5 1.0
C1C A:HEC500 3.0 14.1 1.0
C1D A:HEC500 3.0 16.1 1.0
C4C A:HEC500 3.0 14.9 1.0
C1B A:HEC500 3.0 14.3 1.0
CD2 A:HIS35 3.1 17.7 1.0
C4A A:HEC500 3.1 13.2 1.0
C1A A:HEC500 3.1 14.1 1.0
CE1 A:HIS35 3.1 17.4 1.0
CD A:GLU113 3.2 14.9 1.0
CHD A:HEC500 3.4 14.7 1.0
CHA A:HEC500 3.4 15.0 1.0
CHC A:HEC500 3.5 14.8 1.0
CHB A:HEC500 3.5 14.7 1.0
CG A:GLU113 3.7 15.1 1.0
ND1 A:HIS35 4.2 16.1 1.0
CG A:HIS35 4.2 17.8 1.0
NE2 A:GLN103 4.2 15.5 1.0
OE1 A:GLU113 4.2 15.5 1.0
C2B A:HEC500 4.3 14.6 1.0
OG A:SER107 4.3 13.1 1.0
C3B A:HEC500 4.3 14.8 1.0
C3D A:HEC500 4.3 14.7 1.0
C2D A:HEC500 4.3 15.9 1.0
C3C A:HEC500 4.3 14.4 1.0
C2A A:HEC500 4.3 15.5 1.0
C2C A:HEC500 4.3 13.8 1.0
C3A A:HEC500 4.4 15.2 1.0
CB A:GLU113 4.6 18.0 1.0

Iron binding site 2 out of 4 in 3sjl

Go back to Iron Binding Sites List in 3sjl
Iron binding site 2 out of 4 in the Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:17.1
occ:1.00
FE A:HEC600 0.0 17.1 1.0
NC A:HEC600 1.9 15.6 1.0
OH A:TYR294 2.0 15.1 1.0
NA A:HEC600 2.0 13.3 1.0
NB A:HEC600 2.0 16.8 1.0
ND A:HEC600 2.0 15.5 1.0
NE2 A:HIS205 2.1 14.3 1.0
CZ A:TYR294 3.0 15.6 1.0
C1C A:HEC600 3.0 17.8 1.0
C4C A:HEC600 3.0 14.1 1.0
C1A A:HEC600 3.0 17.1 1.0
C1B A:HEC600 3.0 16.5 1.0
C1D A:HEC600 3.0 14.1 1.0
CE1 A:HIS205 3.0 15.1 1.0
CD2 A:HIS205 3.0 15.2 1.0
C4D A:HEC600 3.0 13.7 1.0
C4A A:HEC600 3.1 17.2 1.0
C4B A:HEC600 3.1 15.7 1.0
CHB A:HEC600 3.4 16.5 1.0
CHD A:HEC600 3.4 14.3 1.0
CHC A:HEC600 3.4 15.3 1.0
CHA A:HEC600 3.5 13.4 1.0
CE1 A:TYR294 3.7 15.2 1.0
CE2 A:TYR294 3.7 16.9 1.0
ND1 A:HIS205 4.1 15.8 1.0
CG A:HIS205 4.2 15.9 1.0
C2C A:HEC600 4.2 16.8 1.0
C2A A:HEC600 4.3 15.4 1.0
C3C A:HEC600 4.3 17.0 1.0
C2B A:HEC600 4.3 17.8 1.0
C3A A:HEC600 4.3 17.1 1.0
C3D A:HEC600 4.3 14.0 1.0
C2D A:HEC600 4.3 13.8 1.0
C3B A:HEC600 4.4 16.8 1.0
CD1 A:TYR294 4.9 16.6 1.0
CD1 A:ILE226 5.0 17.5 1.0
CD2 A:TYR294 5.0 17.3 1.0

Iron binding site 3 out of 4 in 3sjl

Go back to Iron Binding Sites List in 3sjl
Iron binding site 3 out of 4 in the Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:16.6
occ:1.00
FE B:HEC500 0.0 16.6 1.0
ND B:HEC500 2.0 15.5 1.0
NE2 B:HIS35 2.0 14.3 1.0
NA B:HEC500 2.0 15.3 1.0
NB B:HEC500 2.0 14.8 1.0
NC B:HEC500 2.1 16.1 1.0
OE2 B:GLU113 2.1 17.3 1.0
C4D B:HEC500 3.0 13.6 1.0
C4B B:HEC500 3.0 15.5 1.0
CD2 B:HIS35 3.0 16.8 1.0
C1B B:HEC500 3.0 16.4 1.0
CE1 B:HIS35 3.0 14.8 1.0
C4C B:HEC500 3.1 16.4 1.0
C4A B:HEC500 3.1 14.1 1.0
C1A B:HEC500 3.1 16.4 1.0
C1D B:HEC500 3.1 16.3 1.0
C1C B:HEC500 3.1 16.8 1.0
CD B:GLU113 3.2 17.6 1.0
CHA B:HEC500 3.4 12.9 1.0
CHD B:HEC500 3.5 16.5 1.0
CHB B:HEC500 3.5 13.3 1.0
CHC B:HEC500 3.5 16.6 1.0
CG B:GLU113 3.7 18.0 1.0
ND1 B:HIS35 4.2 15.3 1.0
CG B:HIS35 4.2 14.2 1.0
OG B:SER107 4.2 18.0 1.0
NE2 B:GLN103 4.2 16.6 1.0
OE1 B:GLU113 4.2 16.9 1.0
C3B B:HEC500 4.3 16.5 1.0
C3D B:HEC500 4.3 15.8 1.0
C2B B:HEC500 4.3 16.3 1.0
C2D B:HEC500 4.3 14.9 1.0
C3A B:HEC500 4.3 14.9 1.0
C2C B:HEC500 4.3 20.3 1.0
C2A B:HEC500 4.3 14.8 1.0
C3C B:HEC500 4.4 19.2 1.0
CB B:GLU113 4.6 15.4 1.0

Iron binding site 4 out of 4 in 3sjl

Go back to Iron Binding Sites List in 3sjl
Iron binding site 4 out of 4 in the Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the P107S-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:14.1
occ:1.00
FE B:HEC600 0.0 14.1 1.0
OH B:TYR294 1.9 12.5 1.0
NA B:HEC600 2.0 13.1 1.0
ND B:HEC600 2.0 12.7 1.0
NC B:HEC600 2.0 11.1 1.0
NB B:HEC600 2.0 14.1 1.0
NE2 B:HIS205 2.1 14.0 1.0
CZ B:TYR294 2.9 13.9 1.0
C4C B:HEC600 3.0 11.5 1.0
C4A B:HEC600 3.0 13.5 1.0
C1A B:HEC600 3.0 12.3 1.0
C1D B:HEC600 3.0 12.3 1.0
CD2 B:HIS205 3.0 13.0 1.0
C4D B:HEC600 3.0 13.1 1.0
C4B B:HEC600 3.0 14.3 1.0
C1B B:HEC600 3.0 14.3 1.0
C1C B:HEC600 3.0 12.3 1.0
CE1 B:HIS205 3.1 14.2 1.0
CHD B:HEC600 3.4 13.7 1.0
CHA B:HEC600 3.4 9.7 1.0
CHB B:HEC600 3.4 12.8 1.0
CHC B:HEC600 3.5 12.5 1.0
CE1 B:TYR294 3.6 14.8 1.0
CE2 B:TYR294 3.8 12.2 1.0
CG B:HIS205 4.2 13.0 1.0
ND1 B:HIS205 4.2 13.7 1.0
C3A B:HEC600 4.3 14.3 1.0
C3D B:HEC600 4.3 12.3 1.0
C3C B:HEC600 4.3 11.8 1.0
C2D B:HEC600 4.3 14.2 1.0
C2A B:HEC600 4.3 16.4 1.0
C2C B:HEC600 4.3 13.1 1.0
C3B B:HEC600 4.3 13.7 1.0
C2B B:HEC600 4.3 14.8 1.0
CD1 B:TYR294 4.9 12.8 1.0
CD1 B:ILE226 4.9 15.0 1.0
CD2 B:TYR294 5.0 12.4 1.0

Reference:

M.Feng, L.M.Jensen, E.T.Yukl, X.Wei, A.Liu, C.M.Wilmot, V.L.Davidson. Proline 107 Is A Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of Maug. Biochemistry V. 51 1598 2012.
ISSN: ISSN 0006-2960
PubMed: 22299652
DOI: 10.1021/BI201882E
Page generated: Sun Dec 13 15:21:17 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