Chlorine in PDB 3bii: Crystal Structure of Activated Mpt Synthase

The structure of Crystal Structure of Activated Mpt Synthase, PDB code: 3bii was solved by J.N.Daniels, H.Schindelin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	64.796, 48.735, 74.915, 90.00, 107.77, 90.00
R / Rfree (%)	18.9 / 26.1

The binding sites of Chlorine atom in the Crystal Structure of Activated Mpt Synthase (pdb code 3bii). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Activated Mpt Synthase, PDB code: 3bii:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Activated Mpt Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Activated Mpt Synthase within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl303 b:70.3 occ:1.00 O D:HOH310 3.1 24.2 1.0 NE2 D:GLN33 3.1 28.6 1.0 CG D:GLN33 3.5 31.0 1.0 CB D:GLN33 3.6 29.6 1.0 CD D:GLN33 3.6 33.0 1.0 O D:HOH329 4.3 49.3 1.0 CA D:GLN33 4.3 30.0 1.0 O D:GLN33 4.5 29.8 1.0 OE1 D:GLN33 4.7 36.4 1.0 C D:GLN33 4.7 29.8 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Activated Mpt Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Activated Mpt Synthase within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl301 b:43.2 occ:1.00 NH2 E:ARG39 3.1 50.3 1.0 CZ E:ARG39 4.0 51.9 1.0 CE E:LYS119 4.1 41.9 1.0 NH1 E:ARG39 4.2 52.4 1.0 CZ E:PHE34 4.4 25.0 1.0 NZ E:LYS119 4.8 42.2 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Activated Mpt Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Activated Mpt Synthase within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl302 b:49.5 occ:1.00 O E:HOH316 3.0 36.1 1.0 NH2 E:ARG149 3.3 47.5 1.0 OE1 E:GLN112 3.4 38.2 1.0 CG E:GLN112 3.9 37.3 1.0 CD E:GLN112 4.1 38.8 1.0 CB E:GLN112 4.1 35.0 1.0 CZ E:ARG149 4.3 49.6 1.0 NH1 E:ARG149 4.4 49.4 1.0 OD1 E:ASP116 4.6 28.8 1.0 CA E:GLN112 4.8 34.4 1.0 OD2 E:ASP116 4.8 26.6 1.0 O E:HOH342 5.0 37.5 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Activated Mpt Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Activated Mpt Synthase within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl304 b:40.7 occ:1.00 NZ E:LYS126 3.3 29.8 1.0 N E:ARG39 3.3 40.3 1.0 CD1 E:LEU50 3.4 41.4 1.0 CE E:LYS126 3.8 33.2 1.0 CA E:VAL38 3.8 37.3 1.0 CD E:LYS126 3.8 33.8 1.0 O E:HOH336 3.9 33.4 1.0 CG E:ARG39 3.9 44.8 1.0 CG1 E:VAL38 4.1 37.6 1.0 C E:VAL38 4.1 38.6 1.0 CG E:LEU50 4.2 39.4 1.0 CB E:ARG39 4.2 41.9 1.0 CA E:ARG39 4.3 41.5 1.0 O E:ARG39 4.4 41.6 1.0 CB E:VAL38 4.5 37.2 1.0 O E:LYS37 4.6 34.6 1.0 CD2 E:LEU50 4.7 40.0 1.0 C E:ARG39 4.9 41.7 1.0 N E:VAL38 4.9 36.1 1.0 CD E:ARG39 4.9 48.0 1.0 CG2 E:VAL38 5.0 36.4 1.0 O E:HOH365 5.0 27.8 1.0

J.N.Daniels, M.M.Wuebbens, K.V.Rajagopalan, H.Schindelin. Crystal Structure of A Molybdopterin Synthase-Precursor Z Complex: Insight Into Its Sulfur Transfer Mechanism and Its Role in Molybdenum Cofactor Deficiency. Biochemistry V. 47 615 2008.
ISSN: ISSN 0006-2960
PubMed: 18092812
DOI: 10.1021/BI701734G