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Cadmium in PDB 1p8z: Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156

Protein crystallography data

The structure of Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156, PDB code: 1p8z was solved by E.Irobi, L.D.Burtnick, R.C.Robinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.60
Space group P 31 1 2
Cell size a, b, c (Å), α, β, γ (°) 114.220, 114.220, 93.770, 90.00, 90.00, 120.00
R / Rfree (%) 20.8 / 26.3

Other elements in 1p8z:

The structure of Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156 also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156 (pdb code 1p8z). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 3 binding sites of Cadmium where determined in the Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156, PDB code: 1p8z:
Jump to Cadmium binding site number: 1; 2; 3;

Cadmium binding site 1 out of 3 in 1p8z

Go back to Cadmium Binding Sites List in 1p8z
Cadmium binding site 1 out of 3 in the Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cd1002

b:26.4
occ:1.00
O G:ALA116 2.3 21.3 1.0
OE1 A:GLU167 2.5 29.9 1.0
O G:GLY114 2.5 22.8 1.0
OD2 G:ASP109 2.6 29.1 1.0
OD1 G:ASP109 2.9 30.7 1.0
CG G:ASP109 3.1 28.8 1.0
CD A:GLU167 3.4 26.0 1.0
C G:GLY114 3.4 22.9 1.0
C G:ALA116 3.5 23.0 1.0
OE2 A:GLU167 3.6 26.3 1.0
N G:ALA116 3.9 22.0 1.0
CA G:GLY114 3.9 22.6 1.0
CA G:ALA116 4.2 22.3 1.0
C G:ARG115 4.3 23.2 1.0
OE1 G:GLN118 4.4 24.3 1.0
N G:ARG115 4.5 23.6 1.0
N G:VAL117 4.5 23.2 1.0
CB G:ASP109 4.6 26.3 1.0
CA G:VAL117 4.7 24.3 1.0
CA G:ARG115 4.8 24.3 1.0
CG A:GLU167 4.8 24.1 1.0
O G:ARG115 4.9 22.9 1.0
CB G:ALA116 5.0 21.8 1.0

Cadmium binding site 2 out of 3 in 1p8z

Go back to Cadmium Binding Sites List in 1p8z
Cadmium binding site 2 out of 3 in the Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd1001

b:36.5
occ:1.00
O2B A:ATP380 2.5 24.1 1.0
O3G A:ATP380 2.5 24.4 1.0
PB A:ATP380 3.4 23.9 1.0
PG A:ATP380 3.5 28.4 1.0
O3B A:ATP380 3.7 25.3 1.0
O1G A:ATP380 3.7 25.7 1.0
O A:HOH1008 4.0 46.5 1.0
O A:HOH1118 4.1 35.6 1.0
O3A A:ATP380 4.1 23.6 1.0
O1A A:ATP380 4.3 22.5 1.0
CA A:GLY13 4.3 30.2 1.0
PA A:ATP380 4.4 28.1 1.0
NZ A:LYS18 4.5 21.8 1.0
OD2 A:ASP11 4.6 33.5 1.0
OE1 A:GLN137 4.6 23.9 1.0
OD1 A:ASP11 4.6 35.9 1.0
OD2 A:ASP154 4.8 41.0 1.0
O A:HOH1063 4.8 28.1 1.0
O1B A:ATP380 4.8 22.8 1.0
O2G A:ATP380 4.8 28.2 1.0
CD A:GLN137 5.0 23.9 1.0

Cadmium binding site 3 out of 3 in 1p8z

Go back to Cadmium Binding Sites List in 1p8z
Cadmium binding site 3 out of 3 in the Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Complex Between Rabbit Muscle Alpha-Actin: Human Gelsolin Residues VAL26-GLU156 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd1004

b:61.5
occ:1.00
OD1 A:ASP222 2.6 36.4 1.0
OD2 A:ASP222 2.7 37.4 1.0
CG A:ASP222 3.0 35.3 1.0
CB A:GLU224 3.8 39.3 1.0
CB A:ASP222 4.4 33.5 1.0
N A:GLU224 4.5 34.8 1.0
CA A:GLU224 4.7 36.8 1.0
CG A:GLU224 4.8 44.1 1.0
CA A:ASP222 4.9 30.3 1.0
ND2 A:ASN225 4.9 43.6 1.0

Reference:

E.Irobi, L.D.Burtnick, D.Urosev, K.Narayan, R.C.Robinson. From the First to the Second Domain of Gelsolin: A Common Path on the Surface of Actin? Febs Lett. V. 552 86 2003.
ISSN: ISSN 0014-5793
PubMed: 14527665
DOI: 10.1016/S0014-5793(03)00934-7
Page generated: Fri Jul 19 14:04:41 2024

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