Iron in PDB 7li1: Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation

The structure of Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation, PDB code: 7li1 was solved by C.Chan, D.Ng, M.E.Fraser, A.B.Schryvers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.71 / 1.75
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	62.13, 67.56, 73.77, 91.02, 92.26, 105.02
R / Rfree (%)	23.1 / 26.5

The binding sites of Iron atom in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation (pdb code 7li1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation, PDB code: 7li1:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation


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 Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:56.9 occ:1.00 OH A:TYR198 1.9 35.6 1.0 OH A:TYR141 2.0 34.4 1.0 OH A:TYR197 2.1 35.5 1.0 CZ A:TYR198 2.9 36.6 1.0 CZ A:TYR141 3.0 35.3 1.0 CZ A:TYR197 3.1 30.3 1.0 CE1 A:TYR197 3.4 31.8 1.0 O A:HOH565 3.5 49.5 1.0 CE2 A:TYR141 3.5 29.2 1.0 CE2 A:TYR198 3.6 30.6 1.0 CE1 A:TYR198 3.8 37.2 1.0 CE1 A:TYR141 4.1 29.2 1.0 CE2 A:TYR197 4.3 28.6 1.0 O A:HOH562 4.6 39.3 1.0 CD1 A:TYR197 4.8 27.9 1.0 ND2 A:ASN195 4.8 27.3 1.0 CD2 A:TYR198 4.8 29.8 1.0 CD2 A:TYR141 4.9 30.6 1.0 CD1 A:TYR198 4.9 33.5 1.0 NH1 A:ARG101 5.0 30.6 1.0

Iron binding site 2 out of 6 in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation


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 Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe403 b:67.5 occ:1.00 OH B:TYR198 2.0 45.5 1.0 OH B:TYR141 2.0 46.7 1.0 OH B:TYR197 2.2 36.3 1.0 CZ B:TYR198 3.0 39.2 1.0 CZ B:TYR141 3.0 38.4 1.0 CZ B:TYR197 3.3 38.1 1.0 CE2 B:TYR141 3.5 35.0 1.0 CE1 B:TYR197 3.5 35.1 1.0 CE2 B:TYR198 3.6 32.5 1.0 CE1 B:TYR198 4.0 39.6 1.0 O B:HOH506 4.1 44.5 1.0 CE1 B:TYR141 4.1 36.0 1.0 CE2 B:TYR197 4.5 37.5 1.0 CD2 B:TYR141 4.8 33.0 1.0 NH1 B:ARG101 4.8 39.3 1.0 CD2 B:TYR198 4.9 34.8 1.0 CD1 B:TYR197 4.9 34.6 1.0 ND2 B:ASN195 4.9 33.2 1.0

Iron binding site 3 out of 6 in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation


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 Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe403 b:50.0 occ:1.00 OH C:TYR198 2.0 35.0 1.0 OH C:TYR141 2.0 34.5 1.0 OH C:TYR197 2.1 35.2 1.0 CZ C:TYR198 3.0 34.5 1.0 CZ C:TYR141 3.1 34.3 1.0 CZ C:TYR197 3.2 33.1 1.0 CE1 C:TYR197 3.4 34.6 1.0 CE2 C:TYR141 3.5 30.6 1.0 CE2 C:TYR198 3.7 31.6 1.0 CE1 C:TYR198 3.9 35.4 1.0 CE1 C:TYR141 4.2 30.5 1.0 CE2 C:TYR197 4.4 31.4 1.0 O C:HOH527 4.4 33.0 1.0 CD1 C:TYR197 4.8 36.9 1.0 ND2 C:ASN195 4.9 28.7 1.0 CD2 C:TYR141 4.9 30.0 1.0 CD2 C:TYR198 5.0 31.2 1.0

Iron binding site 4 out of 6 in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation


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 Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe403 b:71.1 occ:1.00 OH D:TYR141 3.2 41.8 1.0 FE D:FE404 3.5 79.7 1.0 OH D:TYR198 3.6 38.6 1.0 O D:HOH509 3.7 61.4 1.0 O D:HOH561 3.8 35.1 1.0 O3 D:CO3401 3.8 43.5 1.0 FE D:FE405 3.9 64.7 1.0 NH2 D:ARG135 3.9 29.3 1.0 CZ D:TYR141 3.9 36.0 1.0 CE2 D:TYR141 4.0 33.3 1.0 O1 D:CO3401 4.4 55.0 1.0 C D:CO3401 4.5 48.7 1.0 NH1 D:ARG135 4.7 26.9 1.0 ND2 D:ASN139 4.7 27.0 1.0 CZ D:ARG135 4.7 28.1 1.0 CZ D:TYR198 4.8 36.0 1.0

Iron binding site 5 out of 6 in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe404 b:79.7 occ:1.00 O D:HOH509 3.4 61.4 1.0 FE D:FE403 3.5 71.1 1.0 OH D:TYR141 3.9 41.8 1.0 FE D:FE405 3.9 64.7 1.0 OH D:TYR198 4.7 38.6 1.0 O D:HOH573 4.8 52.6 1.0 O D:ALA8 4.9 43.8 1.0

Iron binding site 6 out of 6 in the Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Holo Moraxella Catarrhalis Ferric Binding Protein A in An Open Conformation within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe405 b:64.7 occ:1.00 OH D:TYR198 1.8 38.6 1.0 OH D:TYR197 2.0 36.3 1.0 OH D:TYR141 2.1 41.8 1.0 CZ D:TYR198 2.8 36.0 1.0 CZ D:TYR197 3.0 35.2 1.0 CZ D:TYR141 3.2 36.0 1.0 CE1 D:TYR197 3.2 37.0 1.0 CE2 D:TYR198 3.5 31.1 1.0 CE2 D:TYR141 3.7 33.3 1.0 CE1 D:TYR198 3.7 35.3 1.0 FE D:FE403 3.9 71.1 1.0 FE D:FE404 3.9 79.7 1.0 CE1 D:TYR141 4.2 31.5 1.0 CE2 D:TYR197 4.3 35.2 1.0 O D:HOH573 4.5 52.6 1.0 CD1 D:TYR197 4.6 36.4 1.0 O D:HOH561 4.7 35.1 1.0 CD2 D:TYR198 4.7 29.9 1.0 ND2 D:ASN195 4.8 29.0 1.0 NH2 D:ARG101 4.8 35.7 1.0 NH1 D:ARG101 4.9 30.7 1.0 CD1 D:TYR198 4.9 30.1 1.0 CD2 D:TYR141 5.0 29.5 1.0

C.Chan, D.Ng, M.E.Fraser, A.B.Schryvers. Structural and Functional Insights Into Iron Acquisition From Lactoferrin and Transferrin in Gram-Negative Bacterial Pathogens. Biometals 2022.
ISSN: ESSN 1572-8773
PubMed: 36418809
DOI: 10.1007/S10534-022-00466-6