Chlorine in PDB 1i6t: Structure of Inorganic Pyrophosphatase

All present enzymatic activity of Structure of Inorganic Pyrophosphatase:
3.6.1.1;

The structure of Structure of Inorganic Pyrophosphatase, PDB code: 1i6t was solved by V.R.Samygina, A.N.Popov, V.S.Lamzin, S.M.Avaeva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 1.20
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	109.356, 109.356, 75.582, 90.00, 90.00, 120.00
R / Rfree (%)	12.9 / 17

The structure of Structure of Inorganic Pyrophosphatase also contains other interesting chemical elements:

Calcium	(Ca)	4 atoms
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Structure of Inorganic Pyrophosphatase (pdb code 1i6t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of Inorganic Pyrophosphatase, PDB code: 1i6t:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Structure of Inorganic Pyrophosphatase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Inorganic Pyrophosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl310 b:32.0 occ:0.60 O A:HOH557 3.1 45.2 1.0 N A:SER111 3.3 25.8 1.0 NE A:ARG88 3.3 34.6 1.0 OG A:SER111 3.4 34.7 0.5 CD2 A:HIS110 3.5 29.0 1.0 O A:HOH463 3.5 37.1 1.0 CD A:ARG88 3.6 31.6 1.0 CG A:HIS110 3.7 26.8 1.0 NE2 A:HIS110 3.8 31.9 1.0 O A:HOH444 3.8 29.0 1.0 CB A:SER111 3.8 29.7 0.5 CA A:HIS110 3.9 21.7 1.0 CB A:SER111 3.9 30.0 0.5 ND1 A:HIS110 4.1 28.2 1.0 C A:HIS110 4.1 22.9 1.0 CE1 A:HIS110 4.1 30.8 1.0 CB A:ARG88 4.1 27.1 1.0 CA A:SER111 4.2 27.2 1.0 CB A:HIS110 4.3 22.4 1.0 CG A:ARG88 4.4 28.3 1.0 O A:HOH630 4.4 44.6 0.5 CZ A:ARG88 4.5 31.2 1.0 OD1 A:ASP118 4.8 35.3 1.0 NH2 A:ARG88 4.9 30.2 1.0

Chlorine binding site 2 out of 3 in the Structure of Inorganic Pyrophosphatase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Inorganic Pyrophosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl311 b:39.1 occ:0.60 O A:HOH648 2.5 31.9 0.5 O A:HOH605 3.0 38.7 0.5 N A:ALA7 3.2 25.8 1.0 ND1 A:HIS60 3.6 37.7 1.0 CA A:PRO6 3.7 29.0 1.0 CB A:ALA7 3.9 26.2 1.0 C A:PRO6 3.9 23.1 1.0 CE1 A:PHE169 4.0 33.5 1.0 CB A:PRO6 4.1 33.5 1.0 CA A:ALA7 4.1 25.2 1.0 CG A:HIS60 4.2 30.1 1.0 CB A:HIS60 4.2 28.8 1.0 O A:HOH544 4.3 35.6 0.5 CZ A:PHE169 4.4 40.2 1.0 CE1 A:HIS60 4.5 38.2 1.0 O A:HOH556 4.5 37.6 0.5 O A:HOH582 4.6 43.0 1.0 N A:GLY8 4.8 27.7 1.0 N A:PRO6 5.0 27.1 1.0

Chlorine binding site 3 out of 3 in the Structure of Inorganic Pyrophosphatase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Inorganic Pyrophosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl312 b:26.4 occ:0.70 O A:HOH452 2.6 23.6 0.6 O A:HOH415 2.8 20.1 1.0 N A:THR75 3.0 16.9 1.0 CA A:PRO74 3.4 16.2 1.0 OD1 A:ASN54 3.5 18.2 1.0 CB A:ALA23 3.5 17.3 1.0 O A:THR75 3.5 18.7 1.0 CA A:CYS53 3.7 16.7 1.0 OG1 A:THR75 3.7 16.4 1.0 O A:VAL73 3.7 16.0 1.0 C A:PRO74 3.7 16.1 1.0 N A:ASN54 3.8 14.6 1.0 CA A:THR75 4.0 17.0 1.0 O A:PRO52 4.1 21.3 1.0 C A:CYS53 4.2 15.3 1.0 C A:THR75 4.2 18.0 1.0 CG A:ASN54 4.2 15.0 1.0 CB A:CYS53 4.3 20.0 1.0 O A:HOH528 4.3 39.1 0.5 CB A:PRO74 4.4 18.1 1.0 N A:PRO74 4.4 16.2 1.0 CB A:THR75 4.4 16.9 1.0 C A:VAL73 4.5 15.1 1.0 O A:HOH479 4.5 31.4 1.0 O A:HOH595 4.5 40.1 0.5 N A:CYS53 4.6 16.9 1.0 ND2 A:ASN54 4.7 12.8 1.0 C A:PRO52 4.8 16.9 1.0 CA A:ALA23 4.9 16.3 1.0 SG A:CYS53 4.9 22.7 1.0 O A:PRO74 4.9 17.8 1.0 CG2 A:THR75 5.0 18.0 1.0

V.R.Samygina, A.N.Popov, E.V.Rodina, N.N.Vorobyeva, V.S.Lamzin, K.M.Polyakov, S.A.Kurilova, T.I.Nazarova, S.M.Avaeva. The Structures of Escherichia Coli Inorganic Pyrophosphatase Complexed with Ca(2+) or Capp(I) at Atomic Resolution and Their Mechanistic Implications. J.Mol.Biol. V. 314 633 2001.
ISSN: ISSN 0022-2836
PubMed: 11846572
DOI: 10.1006/JMBI.2001.5149