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Chlorine in PDB 2izd: Apostreptavidin pH 3.0 I222 Complex

Protein crystallography data

The structure of Apostreptavidin pH 3.0 I222 Complex, PDB code: 2izd was solved by B.A.Katz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.50 / 1.60
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.880, 105.340, 47.400, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 25.2

Other elements in 2izd:

The structure of Apostreptavidin pH 3.0 I222 Complex also contains other interesting chemical elements:

Iodine (I) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Apostreptavidin pH 3.0 I222 Complex (pdb code 2izd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Apostreptavidin pH 3.0 I222 Complex, PDB code: 2izd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2izd

Go back to Chlorine Binding Sites List in 2izd
Chlorine binding site 1 out of 2 in the Apostreptavidin pH 3.0 I222 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Apostreptavidin pH 3.0 I222 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl465

b:40.7
occ:1.00
HG B:SER27 2.0 17.8 1.0
HH B:TYR43 2.0 18.2 1.0
HG B:SER45 2.3 37.5 1.0
HD21 B:ASN23 2.7 24.2 1.0
HE1 B:TYR43 2.8 18.9 1.0
OG B:SER27 2.9 15.9 1.0
OH B:TYR43 3.0 19.6 1.0
H2 B:HOH504 3.2 45.4 1.0
HD13 B:LEU25 3.2 32.0 1.0
OG B:SER45 3.3 38.0 1.0
HB2 B:SER27 3.3 17.9 1.0
HZ2 B:TRP92 3.5 9.0 1.0
CB B:SER27 3.5 16.7 1.0
ND2 B:ASN23 3.5 24.5 1.0
HG21 B:VAL47 3.6 46.4 1.0
HB3 B:SER27 3.6 17.3 1.0
H1 B:HOH504 3.6 44.2 1.0
CE1 B:TYR43 3.6 21.8 1.0
HD22 B:ASN23 3.7 24.1 1.0
CZ B:TYR43 3.7 17.1 1.0
O B:HOH504 3.7 45.5 1.0
H B:ALA46 3.9 37.1 1.0
HA B:SER45 4.0 35.5 1.0
HB2 B:SER45 4.0 36.9 1.0
CB B:SER45 4.2 36.2 1.0
CD1 B:LEU25 4.2 31.5 1.0
HB2 B:LEU25 4.2 26.0 1.0
HD11 B:LEU25 4.2 31.1 1.0
OD2 B:ASP128 4.2 23.9 1.0
CG2 B:VAL47 4.5 45.8 1.0
H B:VAL47 4.5 39.9 1.0
H2 B:HOH507 4.5 37.4 1.0
HG23 B:VAL47 4.5 45.9 1.0
CZ2 B:TRP92 4.5 8.8 1.0
CA B:SER45 4.6 33.6 1.0
CG B:ASN23 4.7 24.0 1.0
HD12 B:LEU25 4.7 31.6 1.0
HE1 B:TRP92 4.8 11.2 1.0
HG22 B:VAL47 4.8 46.4 1.0
HH2 B:TRP79 4.8 22.0 1.0
CD1 B:TYR43 4.9 15.5 1.0
N B:ALA46 4.9 38.4 1.0
OD1 B:ASN23 4.9 29.3 1.0
H1 B:HOH507 5.0 37.4 1.0
CA B:SER27 5.0 17.3 1.0

Chlorine binding site 2 out of 2 in 2izd

Go back to Chlorine Binding Sites List in 2izd
Chlorine binding site 2 out of 2 in the Apostreptavidin pH 3.0 I222 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Apostreptavidin pH 3.0 I222 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl467

b:55.7
occ:1.00
HN1 D:NH4466 1.9 42.9 1.0
HH D:TYR43 2.0 26.3 1.0
HN2 D:NH4466 2.1 43.3 1.0
HG D:SER27 2.2 32.4 1.0
N D:NH4466 2.3 42.3 1.0
HN4 D:NH4466 2.5 43.1 1.0
HG D:SER45 2.8 62.0 1.0
HD21 D:ASN23 2.9 30.4 1.0
OH D:TYR43 3.0 28.6 1.0
HE1 D:TYR43 3.0 20.1 1.0
HD11 D:LEU25 3.1 42.3 0.8
OG D:SER27 3.2 30.4 1.0
HZ2 D:TRP92 3.3 12.6 1.0
HN3 D:NH4466 3.3 42.0 1.0
HD22 D:ASN23 3.4 30.1 1.0
ND2 D:ASN23 3.5 30.3 1.0
OG D:SER45 3.6 63.1 1.0
HB2 D:SER27 3.7 33.5 1.0
HG23 D:VAL47 3.7 65.6 1.0
CE1 D:TYR43 3.7 18.6 1.0
CZ D:TYR43 3.8 21.3 1.0
CB D:SER27 3.8 35.0 1.0
HB3 D:SER27 3.8 33.9 1.0
O D:HOH501 4.2 42.6 1.0
CD1 D:LEU25 4.2 42.5 0.8
OD2 D:ASP128 4.2 29.6 1.0
H D:ALA46 4.2 61.0 1.0
HG21 D:VAL47 4.3 66.0 1.0
H1 D:HOH501 4.3 41.8 1.0
HA D:SER45 4.3 58.2 1.0
CZ2 D:TRP92 4.3 13.3 1.0
CG2 D:VAL47 4.3 65.7 1.0
HG22 D:VAL47 4.4 65.7 1.0
HD12 D:LEU25 4.5 42.0 0.8
HB2 D:LEU25 4.5 39.8 0.8
HB2 D:SER45 4.6 61.7 1.0
HD13 D:LEU25 4.6 41.6 0.8
CB D:SER45 4.6 62.1 1.0
HH2 D:TRP79 4.6 18.5 1.0
H D:VAL47 4.7 66.0 1.0
HE1 D:TRP92 4.7 12.4 1.0
CG D:ASN23 4.7 30.2 1.0
HZ2 D:TRP79 4.9 21.8 1.0
CG D:ASP128 5.0 31.6 1.0

Reference:

B.A.Katz, B.A.Katz. N/A N/A.
ISSN: ISSN 0022-2836
PubMed: 9405158
DOI: 10.1006/JMBI.1997.1444
Page generated: Thu Jul 10 22:58:26 2025

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