Atomistry » Iron » PDB 2ays-2bmm » 2bc5
Atomistry »
  Iron »
    PDB 2ays-2bmm »
      2bc5 »

Iron in PDB 2bc5: Crystal Structure of E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages

Protein crystallography data

The structure of Crystal Structure of E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages, PDB code: 2bc5 was solved by J.Faraone-Mennella, F.A.Tezcan, H.B.Gray, J.R.Winkler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.40 / 2.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.861, 68.158, 90.440, 90.00, 90.00, 90.00
R / Rfree (%) 23.9 / 27.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages (pdb code 2bc5). 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 E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages, PDB code: 2bc5:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 2bc5

Go back to Iron Binding Sites List in 2bc5
Iron binding site 1 out of 4 in the Crystal Structure of E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages


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 E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe150

b:23.6
occ:1.00
FE A:HEM150 0.0 23.6 1.0
ND A:HEM150 2.0 25.5 1.0
NC A:HEM150 2.0 23.9 1.0
NE2 A:HIS102 2.0 28.9 1.0
NB A:HEM150 2.0 17.5 1.0
NA A:HEM150 2.1 24.4 1.0
SD A:MET7 2.4 28.4 1.0
CD2 A:HIS102 2.9 27.5 1.0
C1C A:HEM150 3.0 22.3 1.0
C4B A:HEM150 3.0 20.3 1.0
C4D A:HEM150 3.0 28.2 1.0
C1D A:HEM150 3.0 26.5 1.0
C4C A:HEM150 3.0 25.4 1.0
C1A A:HEM150 3.1 25.9 1.0
CE1 A:HIS102 3.1 30.7 1.0
C1B A:HEM150 3.2 20.9 1.0
C4A A:HEM150 3.2 21.6 1.0
CHC A:HEM150 3.3 21.3 1.0
CHA A:HEM150 3.4 26.6 1.0
CHD A:HEM150 3.4 23.3 1.0
CE A:MET7 3.5 20.1 1.0
CHB A:HEM150 3.6 18.4 1.0
CG A:MET7 3.6 26.2 1.0
CG A:HIS102 4.1 26.2 1.0
ND1 A:HIS102 4.2 29.4 1.0
C2C A:HEM150 4.2 22.2 1.0
C3C A:HEM150 4.2 22.7 1.0
C3D A:HEM150 4.3 31.5 1.0
C2D A:HEM150 4.3 25.6 1.0
C3B A:HEM150 4.3 18.9 1.0
C2A A:HEM150 4.4 31.4 1.0
C2B A:HEM150 4.4 20.9 1.0
CB A:MET7 4.4 28.7 1.0
C3A A:HEM150 4.4 27.2 1.0
NH1 A:ARG106 5.0 40.1 1.0

Iron binding site 2 out of 4 in 2bc5

Go back to Iron Binding Sites List in 2bc5
Iron binding site 2 out of 4 in the Crystal Structure of E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages


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 E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe150

b:20.7
occ:1.00
FE B:HEM150 0.0 20.7 1.0
ND B:HEM150 2.0 18.0 1.0
NE2 B:HIS102 2.0 20.2 1.0
NB B:HEM150 2.0 16.2 1.0
NC B:HEM150 2.1 14.1 1.0
NA B:HEM150 2.1 19.5 1.0
SD B:MET7 2.4 31.6 1.0
CD2 B:HIS102 3.0 18.2 1.0
C4D B:HEM150 3.0 24.4 1.0
C1D B:HEM150 3.0 22.8 1.0
C1A B:HEM150 3.0 25.1 1.0
C4B B:HEM150 3.0 18.1 1.0
CE1 B:HIS102 3.0 19.2 1.0
C1C B:HEM150 3.0 12.8 1.0
C4C B:HEM150 3.1 17.4 1.0
C1B B:HEM150 3.1 22.8 1.0
C4A B:HEM150 3.1 21.8 1.0
CHA B:HEM150 3.3 17.4 1.0
CHC B:HEM150 3.4 16.3 1.0
CHD B:HEM150 3.4 19.2 1.0
CHB B:HEM150 3.5 20.3 1.0
CG B:MET7 3.5 31.6 1.0
CE B:MET7 3.6 35.6 1.0
CG B:HIS102 4.1 19.1 1.0
ND1 B:HIS102 4.1 17.6 1.0
C3D B:HEM150 4.2 23.1 1.0
C2D B:HEM150 4.2 22.1 1.0
C3B B:HEM150 4.3 13.7 1.0
C2C B:HEM150 4.3 16.1 1.0
C2A B:HEM150 4.3 27.9 1.0
C3C B:HEM150 4.3 13.7 1.0
CB B:MET7 4.3 26.4 1.0
C2B B:HEM150 4.3 18.5 1.0
C3A B:HEM150 4.4 26.2 1.0
NH1 B:ARG106 4.8 39.3 1.0

Iron binding site 3 out of 4 in 2bc5

Go back to Iron Binding Sites List in 2bc5
Iron binding site 3 out of 4 in the Crystal Structure of E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages


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 E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe150

b:18.6
occ:1.00
FE C:HEM150 0.0 18.6 1.0
ND C:HEM150 2.0 16.7 1.0
NE2 C:HIS102 2.0 22.5 1.0
NB C:HEM150 2.0 17.1 1.0
NC C:HEM150 2.1 15.0 1.0
NA C:HEM150 2.1 23.4 1.0
SD C:MET7 2.4 16.8 1.0
CD2 C:HIS102 2.9 16.3 1.0
C4D C:HEM150 3.0 22.9 1.0
CE1 C:HIS102 3.0 17.8 1.0
C4B C:HEM150 3.0 18.2 1.0
C1D C:HEM150 3.0 18.6 1.0
C1C C:HEM150 3.0 16.3 1.0
C1B C:HEM150 3.1 18.3 1.0
C1A C:HEM150 3.1 25.6 1.0
C4C C:HEM150 3.1 17.3 1.0
C4A C:HEM150 3.1 22.7 1.0
CHC C:HEM150 3.3 17.1 1.0
CHA C:HEM150 3.4 19.9 1.0
CHD C:HEM150 3.4 14.7 1.0
CHB C:HEM150 3.4 21.1 1.0
CE C:MET7 3.5 23.5 1.0
CG C:MET7 3.6 24.3 1.0
ND1 C:HIS102 4.1 20.5 1.0
CG C:HIS102 4.1 16.0 1.0
C3D C:HEM150 4.2 23.1 1.0
C2D C:HEM150 4.3 18.1 1.0
C3B C:HEM150 4.3 16.4 1.0
C2B C:HEM150 4.3 18.1 1.0
C2C C:HEM150 4.3 17.3 1.0
C3C C:HEM150 4.3 11.6 1.0
C2A C:HEM150 4.4 28.9 1.0
C3A C:HEM150 4.4 25.5 1.0
CB C:MET7 4.4 22.0 1.0

Iron binding site 4 out of 4 in 2bc5

Go back to Iron Binding Sites List in 2bc5
Iron binding site 4 out of 4 in the Crystal Structure of E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages


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 E. Coli Cytochrome B562 with Engineered C-Type Heme Linkages within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe150

b:29.4
occ:1.00
FE D:HEM150 0.0 29.4 1.0
NA D:HEM150 2.0 30.6 1.0
NE2 D:HIS102 2.0 33.6 1.0
ND D:HEM150 2.0 31.2 1.0
NB D:HEM150 2.0 25.9 1.0
NC D:HEM150 2.1 24.3 1.0
SD D:MET7 2.2 29.6 1.0
C1A D:HEM150 3.0 32.8 1.0
CE1 D:HIS102 3.0 33.5 1.0
C4D D:HEM150 3.0 33.3 1.0
CD2 D:HIS102 3.0 34.4 1.0
C4B D:HEM150 3.0 26.5 1.0
C1C D:HEM150 3.0 21.5 1.0
C4A D:HEM150 3.1 30.5 1.0
C1D D:HEM150 3.1 32.6 1.0
C1B D:HEM150 3.1 28.6 1.0
C4C D:HEM150 3.1 27.7 1.0
CHA D:HEM150 3.3 32.1 1.0
CHC D:HEM150 3.3 23.6 1.0
CG D:MET7 3.5 25.6 1.0
CHB D:HEM150 3.5 28.1 1.0
CHD D:HEM150 3.5 28.6 1.0
CE D:MET7 3.5 25.5 1.0
ND1 D:HIS102 4.1 35.0 1.0
CG D:HIS102 4.1 33.6 1.0
C2A D:HEM150 4.2 37.3 1.0
C3D D:HEM150 4.2 36.2 1.0
CB D:MET7 4.3 26.8 1.0
C3A D:HEM150 4.3 36.5 1.0
C2D D:HEM150 4.3 32.2 1.0
C3B D:HEM150 4.3 25.8 1.0
C2C D:HEM150 4.3 23.8 1.0
C2B D:HEM150 4.3 26.8 1.0
C3C D:HEM150 4.4 25.1 1.0
NH1 D:ARG106 5.0 46.1 1.0

Reference:

J.Faraone-Mennella, F.A.Tezcan, H.B.Gray, J.R.Winkler. Stability and Folding Kinetics of Structurally Characterized Cytochrome C-B(562). Biochemistry V. 45 10504 2006.
ISSN: ISSN 0006-2960
PubMed: 16939202
DOI: 10.1021/BI060242X
Page generated: Sun Dec 13 14:40:32 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