Zinc in PDB 1k24: Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis

The structure of Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis, PDB code: 1k24 was solved by S.M.Prince, M.Achtman, J.P.Derrick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.50 / 2.03
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.859, 46.346, 73.977, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 27.4

The binding sites of Zinc atom in the Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis (pdb code 1k24). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis, PDB code: 1k24:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis


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 Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:38.0 occ:1.00 OD2 A:ASP15 2.0 46.6 1.0 NE2 A:HIS13 2.0 36.1 1.0 ND1 A:HIS35 2.0 33.8 1.0 O A:HOH408 2.2 40.9 1.0 CE1 A:HIS35 2.9 36.8 1.0 CG A:ASP15 3.0 40.8 1.0 CD2 A:HIS13 3.0 33.8 1.0 CE1 A:HIS13 3.0 32.9 1.0 CG A:HIS35 3.1 35.4 1.0 OD1 A:ASP15 3.2 41.6 1.0 CB A:HIS35 3.6 34.3 1.0 O A:HOH424 3.8 57.9 1.0 NE2 A:HIS35 4.0 38.6 1.0 ND1 A:HIS13 4.1 33.1 1.0 NH1 A:ARG248 4.1 50.4 1.0 CG A:HIS13 4.1 33.7 1.0 CD2 A:HIS35 4.2 35.2 1.0 NE A:ARG248 4.2 45.2 1.0 CB A:ASP15 4.3 39.8 1.0 CZ A:ARG248 4.5 47.9 1.0 O A:HIS35 4.5 36.6 1.0 C A:HIS35 4.5 34.9 1.0 O A:HOH514 4.6 73.7 1.0 CA A:HIS35 4.7 35.6 1.0 N A:ASP15 4.7 36.5 1.0 N A:ILE36 4.9 34.5 1.0 C A:ILE36 5.0 32.3 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis


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 Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:32.6 occ:0.50 OE1 A:GLU28 1.7 41.5 1.0 ND1 A:HIS30 2.2 34.9 1.0 CD A:GLU28 2.7 44.2 1.0 OE2 A:GLU28 2.9 43.4 1.0 CG A:HIS30 3.0 35.3 1.0 CB A:HIS30 3.1 37.6 1.0 CE1 A:HIS30 3.2 35.4 1.0 N A:HIS30 3.6 45.6 1.0 CA A:HIS30 4.0 42.1 1.0 CG A:GLU28 4.0 50.3 1.0 CD2 A:HIS30 4.2 37.7 1.0 N A:LYS29 4.3 56.3 1.0 NE2 A:HIS30 4.3 37.4 1.0 C A:LYS29 4.7 52.3 1.0 O A:HIS30 4.8 44.4 1.0 C A:HIS30 4.8 43.5 1.0 CA A:GLU28 4.9 59.5 1.0 CA A:LYS29 5.0 58.1 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Opca Outer Membrane Adhesin/Invasin From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:77.3 occ:1.00 OD2 A:ASP69 2.2 0.5 1.0 NE2 A:HIS128 2.2 99.7 1.0 OG1 A:THR176 2.6 0.0 1.0 CG A:ASP69 3.0 0.3 1.0 CD2 A:HIS128 3.1 89.8 1.0 CE1 A:HIS128 3.3 98.7 1.0 OD1 A:ASP69 3.6 0.8 1.0 CB A:LYS127 3.8 0.3 1.0 N A:GLU70 3.8 0.5 1.0 CB A:ASP69 3.8 0.9 1.0 CB A:THR176 3.9 0.1 1.0 OD1 A:ASN177 4.0 0.7 1.0 CG A:LYS127 4.0 0.8 1.0 CA A:ASP69 4.2 0.0 1.0 CA A:THR176 4.2 0.7 1.0 C A:THR176 4.2 0.2 1.0 CG A:HIS128 4.3 83.7 1.0 O A:THR176 4.3 0.2 1.0 ND1 A:HIS128 4.4 89.6 1.0 C A:ASP69 4.5 0.3 1.0 CE A:LYS127 4.6 0.8 1.0 CG A:ASN177 4.6 0.8 1.0 CG2 A:THR176 4.6 96.7 1.0 ND2 A:ASN177 4.7 0.6 1.0 CA A:GLU70 4.8 0.3 1.0 N A:ASN177 4.8 0.5 1.0 CD A:LYS127 4.8 0.4 1.0

S.M.Prince, M.Achtman, J.P.Derrick. Crystal Structure of the Opca Integral Membrane Adhesin From Neisseria Meningitidis. Proc.Natl.Acad.Sci.Usa V. 99 3417 2002.
ISSN: ISSN 0027-8424
PubMed: 11891340
DOI: 10.1073/PNAS.062630899