Zinc in PDB 2bjr: Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B

The structure of Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B, PDB code: 2bjr was solved by R.P.Grant, S.M.Buttery, G.C.Ekman, T.M.Roberts, M.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.8
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.513, 52.954, 95.542, 90.00, 99.17, 90.00
R / Rfree (%)	18.4 / 22.3

The binding sites of Zinc atom in the Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B (pdb code 2bjr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B, PDB code: 2bjr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1369 b:37.2 occ:1.00 NE2 A:HIS86 2.0 36.2 1.0 SG A:CYS179 2.1 37.3 1.0 SG A:CYS174 2.3 37.8 1.0 SG A:CYS176 2.3 41.6 1.0 CE1 A:HIS86 3.0 37.8 1.0 CD2 A:HIS86 3.1 35.0 1.0 CB A:CYS179 3.2 47.5 1.0 CB A:CYS174 3.2 40.8 1.0 CB A:CYS176 3.3 47.3 1.0 N A:CYS176 4.1 47.6 1.0 N A:CYS179 4.1 49.5 1.0 ND1 A:HIS86 4.1 36.4 1.0 CG A:HIS86 4.2 35.3 1.0 CA A:CYS176 4.2 47.6 1.0 CA A:CYS179 4.2 48.0 1.0 O A:HOH2319 4.3 35.3 1.0 CA A:GLY170 4.4 30.8 1.0 CA A:CYS174 4.5 41.0 1.0 O A:CYS176 4.6 48.7 1.0 C A:CYS174 4.6 42.5 1.0 C A:CYS176 4.7 49.0 1.0 N A:GLU175 4.9 44.8 1.0 CD A:PRO171 5.0 29.5 1.0 N A:GLY170 5.0 32.5 1.0 O A:HOH2078 5.0 39.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Nematode Sperm Cell Motility Protein MFP2B within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1369 b:44.9 occ:1.00 NE2 B:HIS86 2.0 40.9 1.0 SG B:CYS179 2.1 55.2 1.0 SG B:CYS174 2.2 50.0 1.0 SG B:CYS176 2.6 52.7 1.0 CE1 B:HIS86 2.9 39.3 1.0 CD2 B:HIS86 3.1 37.2 1.0 CB B:CYS174 3.2 51.4 1.0 CB B:CYS179 3.2 60.7 1.0 CB B:CYS176 3.3 55.5 1.0 ND1 B:HIS86 4.0 37.4 1.0 CG B:HIS86 4.1 37.5 1.0 O B:HOH2206 4.1 51.7 1.0 N B:CYS179 4.2 60.6 1.0 N B:CYS176 4.3 55.2 1.0 CA B:CYS176 4.3 55.6 1.0 CA B:CYS179 4.3 60.9 1.0 CA B:GLY170 4.4 44.1 1.0 CA B:CYS174 4.5 51.3 1.0 O B:HOH2056 4.7 57.7 1.0 C B:CYS174 4.7 52.0 1.0 C B:CYS176 4.7 56.2 1.0 O B:CYS176 4.7 55.6 1.0 CD B:PRO171 4.8 44.0 1.0 O B:CYS174 4.9 51.5 1.0 N B:GLY170 5.0 44.2 1.0

R.P.Grant, S.M.Buttery, G.C.Ekman, T.M.Roberts, M.Stewart. Structure of MFP2 and Its Function in Enhancing Msp Polymerization in Ascaris Sperm Amoeboid Motility J.Mol.Biol. V. 347 583 2005.
ISSN: ISSN 0022-2836
PubMed: 15755452
DOI: 10.1016/J.JMB.2005.01.054