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Chlorine in PDB 1yd6: Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax

Protein crystallography data

The structure of Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax, PDB code: 1yd6 was solved by J.J.Truglio, B.Rhau, D.L.Croteau, L.Wang, M.Skorvaga, E.Karakas, M.J.Dellavecchia, H.Wang, B.Van Houten, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 86.487, 86.660, 67.862, 90.00, 120.16, 90.00
R / Rfree (%) 20.2 / 25.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax (pdb code 1yd6). 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 the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax, PDB code: 1yd6:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 1yd6

Go back to Chlorine Binding Sites List in 1yd6
Chlorine binding site 1 out of 3 in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax


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 the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1001

b:26.5
occ:1.00
ND2 C:ASN80 3.1 22.9 1.0
ND2 B:ASN80 3.2 27.4 1.0
ND2 D:ASN80 3.3 21.6 1.0
ND2 A:ASN80 3.4 25.6 1.0
O D:HOH104 3.6 30.3 1.0
O B:HOH104 3.6 31.6 1.0
OD1 A:ASN80 3.9 25.2 1.0
OD1 D:ASN80 3.9 24.7 1.0
OD1 C:ASN80 4.0 25.9 1.0
CG C:ASN80 4.0 25.4 1.0
OD1 B:ASN80 4.0 27.2 1.0
CG B:ASN80 4.1 29.1 1.0
CG2 C:ILE76 4.1 23.1 1.0
CG A:ASN80 4.1 25.9 1.0
CG D:ASN80 4.1 24.4 1.0
CG2 B:ILE76 4.1 23.6 1.0
CG2 D:ILE76 4.2 23.1 1.0
CG2 A:ILE76 4.2 22.9 1.0

Chlorine binding site 2 out of 3 in 1yd6

Go back to Chlorine Binding Sites List in 1yd6
Chlorine binding site 2 out of 3 in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax


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 the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1005

b:40.5
occ:1.00
NE2 C:HIS85 3.1 27.9 1.0
NZ C:LYS84 3.2 31.3 1.0
CD1 D:LEU75 3.5 29.3 1.0
O C:HOH1051 3.7 59.7 1.0
CD C:LYS84 3.8 27.8 1.0
CE1 C:HIS85 3.8 30.9 1.0
CD2 C:LEU81 3.9 25.6 1.0
CE C:LYS84 3.9 30.4 1.0
CD2 C:LEU20 4.2 31.0 1.0
CD2 C:HIS85 4.2 29.0 1.0
CD1 C:ILE66 4.9 26.8 1.0
CG D:LEU75 4.9 27.6 1.0
CG C:LYS84 5.0 27.7 1.0

Chlorine binding site 3 out of 3 in 1yd6

Go back to Chlorine Binding Sites List in 1yd6
Chlorine binding site 3 out of 3 in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax


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 the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Bacillus Caldotenax within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1006

b:50.8
occ:1.00
OG C:SER36 2.7 24.3 1.0
CB C:SER36 3.6 27.3 1.0
OE2 C:GLU14 3.7 33.6 1.0
CB C:GLU39 3.9 30.5 1.0
CD C:LYS38 3.9 35.7 1.0
CG C:GLU14 4.0 27.2 1.0
N C:GLU39 4.1 29.1 1.0
CD C:GLU14 4.2 28.4 1.0
CB C:LYS38 4.3 27.9 1.0
CG C:LYS38 4.4 33.4 1.0
CA C:GLU39 4.4 30.0 1.0
CB C:GLU14 4.6 24.8 1.0
O C:HOH1028 4.8 35.4 1.0
C C:LYS38 5.0 28.9 1.0
CG C:GLU39 5.0 33.8 1.0
CE C:LYS38 5.0 38.0 1.0

Reference:

J.J.Truglio, B.Rhau, D.L.Croteau, L.Wang, M.Skorvaga, E.Karakas, M.J.Dellavecchia, H.Wang, B.Van Houten, C.Kisker. Structural Insights Into the First Incision Reaction During Nucleotide Excision Repair Embo J. V. 24 885 2005.
ISSN: ISSN 0261-4189
PubMed: 15692561
DOI: 10.1038/SJ.EMBOJ.7600568
Page generated: Thu Jul 10 20:33:39 2025

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