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Iron in PDB 2why: Crystal Structure of the Triscatecholate Siderophore Binding Protein Feua From Bacillus Subtilis Complexed with Ferri-Bacillibactin

Protein crystallography data

The structure of Crystal Structure of the Triscatecholate Siderophore Binding Protein Feua From Bacillus Subtilis Complexed with Ferri-Bacillibactin, PDB code: 2why was solved by F.Peuckert, M.Miethke, A.G.Albrecht, L.-O.Essen, M.A.Marahiel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.51 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.530, 63.140, 55.530, 90.00, 110.44, 90.00
R / Rfree (%) 15.749 / 19.12

Other elements in 2why:

The structure of Crystal Structure of the Triscatecholate Siderophore Binding Protein Feua From Bacillus Subtilis Complexed with Ferri-Bacillibactin also contains other interesting chemical elements:

Chlorine (Cl) 11 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Triscatecholate Siderophore Binding Protein Feua From Bacillus Subtilis Complexed with Ferri-Bacillibactin (pdb code 2why). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of the Triscatecholate Siderophore Binding Protein Feua From Bacillus Subtilis Complexed with Ferri-Bacillibactin, PDB code: 2why:

Iron binding site 1 out of 1 in 2why

Go back to Iron Binding Sites List in 2why
Iron binding site 1 out of 1 in the Crystal Structure of the Triscatecholate Siderophore Binding Protein Feua From Bacillus Subtilis Complexed with Ferri-Bacillibactin


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 Triscatecholate Siderophore Binding Protein Feua From Bacillus Subtilis Complexed with Ferri-Bacillibactin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1001

b:19.8
occ:1.00
O3 B:DBH21 1.9 22.3 1.0
O6 B:DBH31 2.0 21.7 1.0
O3 B:DBH11 2.1 19.6 1.0
O6 B:DBH11 2.1 20.0 1.0
O3 B:DBH31 2.1 20.4 1.0
O6 B:DBH21 2.1 20.7 1.0
C3 B:DBH21 2.8 22.2 1.0
C6 B:DBH21 2.8 20.7 1.0
C6 B:DBH31 2.9 22.4 1.0
C3 B:DBH31 2.9 20.3 1.0
C6 B:DBH11 2.9 21.6 1.0
C3 B:DBH11 2.9 21.9 1.0
NE2 A:GLN215 3.9 24.4 1.0
NH1 A:ARG180 3.9 23.1 1.0
NZ A:LYS84 4.0 26.5 1.0
O B:HOH2002 4.0 19.2 1.0
O B:HOH2007 4.0 31.0 1.0
O B:HOH2003 4.1 26.6 1.0
C18 B:DBH21 4.1 21.3 1.0
O B:HOH2008 4.1 24.7 1.0
C9 B:DBH31 4.2 22.5 1.0
C9 B:DBH21 4.2 20.5 1.0
C9 B:DBH11 4.2 22.0 1.0
C18 B:DBH11 4.2 21.9 1.0
C18 B:DBH31 4.2 21.7 1.0
NZ A:LYS105 4.3 26.0 1.0
CD A:LYS105 4.3 26.6 1.0
SD A:MET85 4.5 29.9 0.3
CE A:LYS84 4.6 27.2 1.0
N B:GLY22 4.6 26.1 1.0
CE A:LYS105 4.7 25.8 1.0
N B:GLY12 4.7 27.4 1.0
CZ A:ARG180 4.7 24.1 1.0
C21 B:DBH21 4.8 24.5 1.0
CE A:MET85 4.9 32.5 0.7
N B:GLY32 4.9 26.0 1.0
NH2 A:ARG180 4.9 23.7 1.0
C21 B:DBH11 4.9 24.9 1.0
CD A:GLN215 4.9 22.0 1.0
C21 B:DBH31 5.0 24.1 1.0

Reference:

F.Peuckert, M.Miethke, A.G.Albrecht, L.-O.Essen, M.A.Marahiel. Structural Basis and Stereochemistry of Triscatecholate Siderophore Binding By Feua. Angew.Chem.Int.Ed.Engl. V. 48 7924 2009.
ISSN: ISSN 1433-7851
PubMed: 19746494
DOI: 10.1002/ANIE.200902495
Page generated: Thu Jul 17 05:02:30 2025

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