Iron in PDB 3ve1: The 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin

The structure of The 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin, PDB code: 3ve1 was solved by C.Calmettes, T.F.Moraes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.93 / 2.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	128.023, 153.509, 169.511, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 24.9

The binding sites of Iron atom in the The 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin (pdb code 3ve1). 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 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin, PDB code: 3ve1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe702 b:43.2 occ:1.00 OH B:TYR517 2.1 58.9 1.0 OD1 B:ASP392 2.1 51.5 1.0 O3 B:CO3701 2.1 36.5 1.0 NE2 B:HIS585 2.2 47.1 1.0 O1 B:CO3701 2.3 36.5 1.0 OH B:TYR426 2.4 61.9 1.0 C B:CO3701 2.5 36.5 1.0 CZ B:TYR517 3.1 59.2 1.0 CE1 B:HIS585 3.1 46.8 1.0 CD2 B:HIS585 3.2 47.4 1.0 CG B:ASP392 3.3 50.7 1.0 CZ B:TYR426 3.4 63.5 1.0 CE1 B:TYR517 3.6 60.0 1.0 CE2 B:TYR426 3.7 64.4 1.0 O2 B:CO3701 3.8 36.5 1.0 NH2 B:ARG456 4.1 52.3 1.0 CB B:ASP392 4.1 49.9 1.0 CE2 B:TYR517 4.2 59.1 1.0 OD2 B:ASP392 4.2 50.7 1.0 NH1 B:ARG632 4.2 54.4 1.0 ND1 B:HIS585 4.3 46.9 1.0 CG B:HIS585 4.4 47.4 1.0 CB B:THR457 4.4 50.4 1.0 CE1 B:TYR426 4.5 64.4 1.0 OG1 B:THR457 4.6 49.5 1.0 NE B:ARG456 4.7 51.2 1.0 CA B:ASP392 4.7 50.3 1.0 N B:ALA458 4.7 52.3 1.0 N B:THR457 4.8 48.5 1.0 CZ B:ARG456 4.9 51.6 1.0 CD1 B:TYR517 5.0 60.5 1.0

Iron binding site 2 out of 2 in the The 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The 2.9 Angstrom Crystal Structure of Transferrin Binding Protein B (Tbpb) From Serogroup B M982 Neisseria Meningitidis in Complex with Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe702 b:44.6 occ:1.00 OD1 D:ASP392 2.0 58.4 1.0 NE2 D:HIS585 2.2 51.9 1.0 OH D:TYR426 2.2 43.0 1.0 O1 D:CO3701 2.2 48.5 1.0 OH D:TYR517 2.2 49.8 1.0 O3 D:CO3701 2.2 48.5 1.0 C D:CO3701 2.6 48.5 1.0 CD2 D:HIS585 3.1 52.1 1.0 CE1 D:HIS585 3.1 49.4 1.0 CZ D:TYR426 3.2 43.9 1.0 CG D:ASP392 3.3 57.4 1.0 CZ D:TYR517 3.3 49.8 1.0 O D:HOH803 3.6 30.8 1.0 CE2 D:TYR426 3.6 45.6 1.0 O2 D:CO3701 3.9 48.5 1.0 CE1 D:TYR517 3.9 53.2 1.0 CB D:ASP392 4.1 53.2 1.0 OD2 D:ASP392 4.1 60.0 1.0 CB D:THR457 4.2 49.6 1.0 NH1 D:ARG632 4.3 50.1 1.0 ND1 D:HIS585 4.3 48.8 1.0 CG D:HIS585 4.3 49.8 1.0 CE1 D:TYR426 4.3 43.4 1.0 NH2 D:ARG456 4.4 44.3 1.0 OG1 D:THR457 4.4 47.0 1.0 CE2 D:TYR517 4.4 47.3 1.0 CA D:ASP392 4.6 52.7 1.0 N D:ALA458 4.7 59.1 1.0 N D:THR457 4.8 46.1 1.0 NE D:ARG456 4.8 46.0 1.0 CD2 D:TYR426 5.0 46.2 1.0 N D:GLY393 5.0 36.9 1.0 CA D:THR457 5.0 51.0 1.0

C.Calmettes, J.Alcantara, R.H.Yu, A.B.Schryvers, T.F.Moraes. The Structural Basis of Transferrin Sequestration By Transferrin-Binding Protein B. Nat.Struct.Mol.Biol. V. 19 358 2012.
ISSN: ISSN 1545-9993
PubMed: 22343719
DOI: 10.1038/NSMB.2251