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Chlorine in PDB 2cz4: Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8

Protein crystallography data

The structure of Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8, PDB code: 2cz4 was solved by R.Arai, E.Fusatomi, M.Kukimoto-Niino, S.Kawaguchi, T.Terada, M.Shirouzu, S.Yokoyama, Riken Structural Genomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.11 / 1.93
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 61.345, 117.699, 114.114, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 22.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8 (pdb code 2cz4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8, PDB code: 2cz4:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 2cz4

Go back to Chlorine Binding Sites List in 2cz4
Chlorine binding site 1 out of 3 in the Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8


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 A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:25.4
occ:1.00
O A:HOH341 2.8 38.0 1.0
NZ A:LYS7 3.1 18.9 1.0
O C:HOH351 3.3 60.0 1.0
CB A:ASN90 3.9 17.4 1.0
N A:ASN90 3.9 16.7 1.0
CE A:LYS7 4.0 18.8 1.0
CD A:LYS7 4.1 14.8 1.0
CA A:ASN90 4.3 15.3 1.0
O C:HOH325 4.3 31.9 1.0
C A:GLU89 4.4 17.7 1.0
CD1 C:TRP92 4.6 17.3 1.0
CG A:ASN90 4.7 22.3 1.0
OD1 A:ASN90 4.7 17.8 1.0
CA A:GLU89 4.7 17.6 1.0
O A:GLU89 4.9 16.0 1.0
O A:VAL88 5.0 16.6 1.0

Chlorine binding site 2 out of 3 in 2cz4

Go back to Chlorine Binding Sites List in 2cz4
Chlorine binding site 2 out of 3 in the Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8


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 A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl202

b:30.3
occ:1.00
NZ B:LYS7 3.1 19.5 1.0
O A:HOH361 3.4 57.0 1.0
CE B:LYS7 3.9 19.9 1.0
CB B:ASN90 3.9 22.5 1.0
N B:ASN90 4.1 19.3 1.0
CD B:LYS7 4.1 18.9 1.0
CA B:ASN90 4.3 19.1 1.0
C B:GLU89 4.4 25.0 1.0
O B:HOH315 4.5 28.8 1.0
CD1 A:TRP92 4.5 16.6 1.0
OD1 B:ASN90 4.6 20.1 1.0
CG B:ASN90 4.7 24.4 1.0
O B:GLU89 4.9 17.5 1.0
CA B:GLU89 4.9 22.0 1.0
O B:VAL88 4.9 17.0 1.0

Chlorine binding site 3 out of 3 in 2cz4

Go back to Chlorine Binding Sites List in 2cz4
Chlorine binding site 3 out of 3 in the Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8


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 A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl203

b:26.2
occ:1.00
NZ C:LYS7 3.1 18.5 1.0
O B:HOH334 3.6 45.2 1.0
CE C:LYS7 3.9 16.6 1.0
CB C:ASN90 3.9 22.9 1.0
N C:ASN90 4.0 22.2 1.0
CD C:LYS7 4.1 16.7 1.0
CA C:ASN90 4.3 20.7 1.0
C C:GLU89 4.3 22.4 1.0
O C:HOH311 4.5 33.0 1.0
CD1 B:TRP92 4.6 18.0 1.0
OD1 C:ASN90 4.6 19.9 1.0
CG C:ASN90 4.7 23.2 1.0
O C:GLU89 4.8 21.1 1.0
CA C:GLU89 4.8 21.0 1.0

Reference:

R.Arai, E.Fusatomi, M.Kukimoto-Niino, S.Kawaguchi, T.Terada, M.Shirouzu, S.Yokoyama. Crystal Structure of A Putative Pii-Like Signaling Protein (TTHA0516) From Thermus Thermophilus HB8 To Be Published.
Page generated: Sat Jul 20 06:25:11 2024

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