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Antimony in PDB 1f48: Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase

Protein crystallography data

The structure of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase, PDB code: 1f48 was solved by T.Zhou, S.Radaev, B.P.Rosen, D.L.Gatti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.37 / 2.30
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.523, 75.715, 222.714, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26.3

Antimony Binding Sites:

The binding sites of Antimony atom in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase (pdb code 1f48). This binding sites where shown within 5.0 Angstroms radius around Antimony atom.
In total 4 binding sites of Antimony where determined in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase, PDB code: 1f48:
Jump to Antimony binding site number: 1; 2; 3; 4;

Antimony binding site 1 out of 4 in 1f48

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Antimony binding site 1 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase


Mono view


Stereo pair view

A full contact list of Antimony with other atoms in the Sb binding site number 1 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sb594

b:40.0
occ:1.00
SG A:CYS113 2.6 35.5 1.0
SG A:CYS422 2.6 39.6 1.0
CL A:CL597 2.6 32.6 1.0
SG A:CYS172 2.7 33.1 1.0
O A:HOH717 2.8 28.4 1.0
CB A:CYS113 3.6 29.4 1.0
CB A:CYS422 3.6 39.4 1.0
CB A:CYS172 3.7 37.5 1.0
CB A:SER420 3.7 38.6 1.0
SB A:SB595 3.7 36.5 1.0
OG A:SER420 3.8 42.4 1.0
O A:HOH841 3.9 32.4 1.0
SB A:SB596 4.3 39.1 1.0
N A:CYS113 4.4 28.8 1.0
N A:CYS422 4.5 37.5 1.0
CA A:CYS113 4.6 30.2 1.0
CA A:CYS422 4.7 41.2 1.0
O A:HOH862 4.9 43.9 1.0

Antimony binding site 2 out of 4 in 1f48

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Antimony binding site 2 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase


Mono view


Stereo pair view

A full contact list of Antimony with other atoms in the Sb binding site number 2 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sb595

b:36.5
occ:1.00
NE2 A:HIS453 2.4 31.8 1.0
SG A:CYS172 2.6 33.1 1.0
O A:HOH720 2.6 36.8 1.0
CL A:CL598 2.7 31.6 1.0
CL A:CL597 2.8 32.6 1.0
CE1 A:HIS453 3.3 29.9 1.0
CD2 A:HIS453 3.4 30.0 1.0
O A:HOH841 3.4 32.4 1.0
CB A:CYS172 3.5 37.5 1.0
SB A:SB594 3.7 40.0 1.0
CA A:CYS172 4.0 38.1 1.0
CD2 A:LEU457 4.0 40.8 1.0
CA A:GLY111 4.1 25.0 1.0
O A:GLN108 4.3 38.2 1.0
O A:SER171 4.4 43.9 1.0
N A:GLY111 4.4 34.4 1.0
ND1 A:HIS453 4.4 34.3 1.0
CG A:HIS453 4.5 34.3 1.0
CB A:CYS113 4.5 29.4 1.0
N A:CYS172 4.7 41.0 1.0
C A:GLY111 4.8 30.8 1.0
C A:SER171 4.9 50.6 1.0

Antimony binding site 3 out of 4 in 1f48

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Antimony binding site 3 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase


Mono view


Stereo pair view

A full contact list of Antimony with other atoms in the Sb binding site number 3 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sb596

b:39.1
occ:1.00
OG A:SER420 2.3 42.4 1.0
NE2 A:HIS148 2.4 30.9 1.0
CL A:CL599 2.5 54.7 1.0
O A:HOH788 2.6 25.9 1.0
SG A:CYS113 2.6 35.5 1.0
CD2 A:HIS148 3.3 25.7 1.0
CB A:CYS113 3.4 29.4 1.0
CB A:SER420 3.4 38.6 1.0
CE1 A:HIS148 3.5 26.7 1.0
O A:HOH802 3.8 46.0 1.0
CD1 A:LEU152 4.0 25.9 1.0
O A:HOH727 4.1 36.4 1.0
CA A:SER420 4.1 36.6 1.0
CB A:CYS172 4.1 37.5 1.0
SB A:SB594 4.3 40.0 1.0
CG A:HIS148 4.5 29.7 1.0
CA A:CYS113 4.5 30.2 1.0
ND1 A:HIS148 4.6 29.0 1.0
OD1 A:ASP417 4.6 37.6 1.0
O A:CYS172 4.7 38.6 1.0
O A:ASP417 4.9 29.5 1.0
N A:SER420 4.9 36.8 1.0
SG A:CYS172 5.0 33.1 1.0

Antimony binding site 4 out of 4 in 1f48

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Antimony binding site 4 out of 4 in the Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase


Mono view


Stereo pair view

A full contact list of Antimony with other atoms in the Sb binding site number 4 of Crystal Structure of the Escherichia Coli Arsenite-Translocating Atpase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sb701

b:93.6
occ:0.50
SB A:SBO701 0.0 93.6 0.5
O2 A:SBO701 1.9 73.5 0.5
O1 A:SBO701 2.1 78.6 0.5
O3 A:SBO701 2.1 75.2 0.5
NH2 A:ARG543 3.1 52.8 1.0
NH2 A:ARG206 3.6 63.8 1.0
O4' A:ADP590 3.8 35.9 1.0
CZ A:ARG543 4.0 50.5 1.0
N3 A:ADP590 4.1 46.5 1.0
NH1 A:ARG206 4.1 62.2 1.0
C4 A:ADP590 4.2 43.4 1.0
N9 A:ADP590 4.3 42.9 1.0
CZ A:ARG206 4.3 64.4 1.0
C1' A:ADP590 4.3 41.0 1.0
NE A:ARG543 4.4 53.3 1.0
C2 A:ADP590 4.6 43.5 1.0
OD1 A:ASN281 4.8 44.2 1.0
C4' A:ADP590 4.8 44.4 1.0
CD A:GLU500 4.8 47.7 1.0
C5 A:ADP590 4.9 40.9 1.0
NH1 A:ARG543 4.9 46.0 1.0
CG A:GLU500 4.9 41.2 1.0
CD1 A:LEU277 4.9 38.4 1.0
C8 A:ADP590 5.0 43.6 1.0
OE1 A:GLU500 5.0 51.4 1.0

Reference:

T.Zhou, S.Radaev, B.P.Rosen, D.L.Gatti. Structure of the Arsa Atpase: the Catalytic Subunit of A Heavy Metal Resistance Pump. Embo J. V. 19 4838 2000.
ISSN: ISSN 0261-4189
PubMed: 10970874
DOI: 10.1093/EMBOJ/19.17.4838
Page generated: Fri Sep 25 14:36:39 2020
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