Platinum in PDB 2pil: Crystallographic Structure of Phosphorylated Pilin From Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry

The structure of Crystallographic Structure of Phosphorylated Pilin From Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry, PDB code: 2pil was solved by K.T.Forest, S.A.Dunham, M.Koomey, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	127.580, 121.080, 26.860, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / n/a

The binding sites of Platinum atom in the Crystallographic Structure of Phosphorylated Pilin From Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry (pdb code 2pil). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total only one binding site of Platinum was determined in the Crystallographic Structure of Phosphorylated Pilin From Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry, PDB code: 2pil:

Platinum binding site 1 out of 1 in the Crystallographic Structure of Phosphorylated Pilin From Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Crystallographic Structure of Phosphorylated Pilin From Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt200 b:86.5 occ:1.00 O A:HOH810 1.4 0.0 1.0 O A:HOH333 2.7 90.3 1.0 NE2 A:HIS54 3.3 35.7 1.0 CD2 A:HIS54 3.8 39.2 1.0 CE1 A:HIS54 4.0 37.9 1.0 CG A:HIS54 4.7 36.6 1.0 ND1 A:HIS54 4.8 45.7 1.0 OH A:TYR50 5.0 35.5 1.0

K.T.Forest, S.A.Dunham, M.Koomey, J.A.Tainer. Crystallographic Structure Reveals Phosphorylated Pilin From Neisseria: Phosphoserine Sites Modify Type IV Pilus Surface Chemistry and Fibre Morphology. Mol.Microbiol. V. 31 743 1999.
ISSN: ISSN 0950-382X
PubMed: 10048019
DOI: 10.1046/J.1365-2958.1999.01184.X