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Iodine in PDB 5nfi: The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis

Protein crystallography data

The structure of The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis, PDB code: 5nfi was solved by M.Hall, Y.Hasegawa, K.Persson, F.Yoshimura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.61 / 2.51
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 101.600, 83.210, 38.740, 90.00, 94.76, 90.00
R / Rfree (%) 19.7 / 26.3

Iodine Binding Sites:

The binding sites of Iodine atom in the The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis (pdb code 5nfi). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis, PDB code: 5nfi:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in 5nfi

Go back to Iodine Binding Sites List in 5nfi
Iodine binding site 1 out of 2 in the The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:I401

b:57.4
occ:0.80
CG2 B:VAL83 3.5 50.6 1.0
OH B:TYR70 3.5 48.6 1.0
CE1 B:TYR70 3.9 49.2 1.0
CD1 B:ILE122 4.0 54.2 1.0
ND2 B:ASN68 4.0 52.1 1.0
CZ B:TYR70 4.1 48.5 1.0
CB B:ALA81 4.4 56.0 1.0
CG2 B:ILE122 4.8 57.3 1.0
C B:ALA81 4.8 56.4 1.0
N B:ASN82 4.9 55.5 1.0
O B:ASN82 4.9 55.1 1.0
CB B:VAL83 5.0 51.4 1.0
O B:ALA81 5.0 57.4 1.0
C B:ASN82 5.0 56.3 1.0

Iodine binding site 2 out of 2 in 5nfi

Go back to Iodine Binding Sites List in 5nfi
Iodine binding site 2 out of 2 in the The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of The Fimbrial Anchor Protein MFA2 From Porphyromonas Gingivalis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:I402

b:54.6
occ:0.59
OH B:TYR198 3.2 60.4 1.0
N B:TYR305 3.5 61.0 1.0
OG1 B:THR304 3.7 0.1 1.0
CG2 B:ILE263 3.7 58.9 1.0
CE2 B:TYR198 3.8 57.8 1.0
CZ B:TYR198 4.0 58.5 1.0
CG2 B:THR304 4.0 0.0 1.0
CA B:THR304 4.1 65.6 1.0
CB B:THR304 4.1 0.5 1.0
CD B:ARG261 4.3 72.6 1.0
C B:THR304 4.3 63.9 1.0
CG B:HIS256 4.4 51.7 1.0
CB B:TYR305 4.4 57.8 1.0
CB B:HIS256 4.4 52.4 1.0
CD2 B:HIS256 4.4 51.3 1.0
CA B:TYR305 4.5 59.3 1.0
CD1 B:TYR305 4.5 60.0 1.0
O B:TYR305 4.6 58.9 1.0
NE B:ARG261 4.6 75.2 1.0
CD1 B:ILE263 4.9 58.1 1.0
CB B:ILE263 4.9 58.4 1.0
CG B:TYR305 5.0 59.3 1.0
ND1 B:HIS256 5.0 51.9 1.0
C B:TYR305 5.0 58.8 1.0

Reference:

M.Hall, Y.Hasegawa, F.Yoshimura, K.Persson. Structural and Functional Characterization of Shaft, Anchor, and Tip Proteins of the MFA1 Fimbria From the Periodontal Pathogen Porphyromonas Gingivalis. Sci Rep V. 8 1793 2018.
ISSN: ESSN 2045-2322
PubMed: 29379120
DOI: 10.1038/S41598-018-20067-Z
Page generated: Sun Aug 11 21:38:37 2024

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