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Iron in PDB 5oah: The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin

Protein crystallography data

The structure of The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin, PDB code: 5oah was solved by A.D.J.Raines, E.Blagova, E.J.Dodson, K.S.Wilson, A.K.Duhme-Klair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.52 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 58.139, 63.410, 67.674, 82.71, 76.36, 79.03
R / Rfree (%) 20.5 / 25.1

Iron Binding Sites:

The binding sites of Iron atom in the The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin (pdb code 5oah). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin, PDB code: 5oah:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5oah

Go back to Iron Binding Sites List in 5oah
Iron binding site 1 out of 2 in the The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:39.6
occ:1.00
OAG A:95B402 2.0 35.1 1.0
OH A:TYR288 2.0 34.2 1.0
NE2 A:HIS227 2.0 82.5 1.0
OAF A:95B402 2.1 41.2 1.0
OAE A:95B402 2.1 32.8 1.0
OAH A:95B402 2.1 43.5 1.0
CE1 A:HIS227 2.9 85.8 1.0
CAZ A:95B402 2.9 37.2 1.0
CAX A:95B402 2.9 33.6 1.0
CAY A:95B402 3.0 53.5 1.0
CBA A:95B402 3.0 47.9 1.0
CZ A:TYR288 3.1 40.7 1.0
CD2 A:HIS227 3.2 90.3 1.0
NH2 A:ARG249 3.5 61.0 1.0
CE2 A:TYR288 3.8 37.9 1.0
CE1 A:TYR288 4.0 39.5 1.0
ND1 A:HIS227 4.0 94.8 1.0
NH1 A:ARG205 4.2 44.3 1.0
NE2 A:GLN98 4.2 46.8 1.0
CBB A:95B402 4.2 40.2 1.0
NH2 A:ARG118 4.2 37.3 1.0
CAK A:95B402 4.3 36.1 1.0
NE A:ARG118 4.3 35.1 1.0
CG A:HIS227 4.3 93.8 1.0
CAL A:95B402 4.3 54.5 1.0
CBC A:95B402 4.3 59.2 1.0
NE A:ARG249 4.4 45.6 1.0
NAS A:95B402 4.4 46.3 1.0
CZ A:ARG249 4.4 55.9 1.0
NH2 A:ARG205 4.6 41.0 1.0
N A:95B402 4.7 59.4 1.0
CZ A:ARG118 4.7 38.3 1.0
CAV A:95B402 4.9 47.1 1.0
CAP A:95B402 4.9 58.7 1.0
CZ A:ARG205 4.9 42.1 1.0

Iron binding site 2 out of 2 in 5oah

Go back to Iron Binding Sites List in 5oah
Iron binding site 2 out of 2 in the The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Periplasmic Binding Protein Ceue of Campylobacter Jejuni Binds the Iron(III) Complex of Azotochelin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe401

b:31.6
occ:1.00
OAH B:95B402 2.0 35.2 1.0
OAE B:95B402 2.0 28.1 1.0
NE2 B:HIS227 2.0 42.2 1.0
OAF B:95B402 2.0 34.6 1.0
OAG B:95B402 2.1 30.8 1.0
OH B:TYR288 2.1 32.0 1.0
CAX B:95B402 2.8 30.7 1.0
CBA B:95B402 2.8 34.9 1.0
CAY B:95B402 2.8 38.5 1.0
CAZ B:95B402 2.9 32.1 1.0
CE1 B:HIS227 2.9 40.8 1.0
CZ B:TYR288 3.1 30.8 1.0
CD2 B:HIS227 3.2 41.1 1.0
NH2 B:ARG249 3.6 76.1 1.0
CE2 B:TYR288 3.8 28.2 1.0
CE1 B:TYR288 4.0 32.4 1.0
ND1 B:HIS227 4.1 43.6 1.0
CAK B:95B402 4.2 28.8 1.0
NH1 B:ARG205 4.2 26.5 1.0
CAL B:95B402 4.2 42.7 1.0
CBC B:95B402 4.2 45.9 1.0
NE2 B:GLN98 4.2 50.8 1.0
NH2 B:ARG118 4.2 33.6 1.0
CBB B:95B402 4.2 36.9 1.0
NE B:ARG249 4.2 59.8 1.0
CG B:HIS227 4.3 46.8 1.0
NE B:ARG118 4.3 30.0 1.0
CZ B:ARG249 4.4 64.3 1.0
N B:95B402 4.6 58.2 1.0
NAS B:95B402 4.6 50.6 1.0
NH2 B:ARG205 4.7 28.8 1.0
CZ B:ARG118 4.7 33.2 1.0
CZ B:ARG205 4.9 26.9 1.0
CAW B:95B402 4.9 55.9 1.0
CAV B:95B402 5.0 44.0 1.0

Reference:

A.D.J.Raines, J.E.Clarke, E.Blagova, E.J.Dodson, K.S.Wilson, A.K.Duhme-Klair. Redox-Switchable Siderophore Anchor Enables Reversible Artificial Metalloenzyme Assembly Nat Catal 2018.
DOI: 10.1038/S41929-018-0124-3
Page generated: Sun Dec 13 16:09:48 2020

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