Zinc in PDB 8j48: Crystal Structure of Ga

Protein crystallography data

The structure of Crystal Structure of Ga, PDB code: 8j48 was solved by C.Dong, X.Yan, X.Yuan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.70 / 1.94
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 35.835, 73.397, 58.671, 90, 107.22, 90
R / Rfree (%) 20.2 / 23.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Ga (pdb code 8j48). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Ga, PDB code: 8j48:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8j48

Go back to Zinc Binding Sites List in 8j48
Zinc binding site 1 out of 2 in the Crystal Structure of Ga


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Ga within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn201

b:30.8
occ:0.00
SG D:CYS179 2.2 33.1 1.0
SG D:CYS176 2.2 27.0 1.0
SG D:CYS154 2.2 30.7 1.0
SG D:CYS157 2.3 31.9 1.0
CB D:CYS154 3.1 27.7 1.0
CB D:CYS179 3.2 23.2 1.0
CB D:CYS157 3.2 30.8 1.0
CB D:CYS176 3.2 30.4 1.0
N D:CYS157 3.6 36.5 1.0
N D:CYS176 3.7 23.7 1.0
CA D:CYS157 3.9 37.2 1.0
O D:HOH301 4.0 48.7 1.0
CA D:CYS176 4.0 27.7 1.0
CG2 D:THR159 4.2 29.0 1.0
O B:HOH278 4.3 37.7 1.0
N D:CYS179 4.3 24.2 1.0
CA D:CYS179 4.3 23.4 1.0
CA D:CYS154 4.5 30.7 1.0
C D:CYS157 4.6 39.0 1.0
N D:ASP158 4.6 35.0 1.0
C D:CYS176 4.7 22.5 1.0
C D:ASN156 4.8 39.1 1.0
CB D:ASN156 4.8 36.7 1.0
O D:CYS176 4.9 19.8 1.0
C D:LEU175 4.9 26.9 1.0
N D:THR159 5.0 37.3 1.0
O D:HOH318 5.0 33.1 1.0

Zinc binding site 2 out of 2 in 8j48

Go back to Zinc Binding Sites List in 8j48
Zinc binding site 2 out of 2 in the Crystal Structure of Ga


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Ga within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:32.6
occ:0.00
SG A:CYS179 2.1 31.2 1.0
SG A:CYS154 2.2 33.8 1.0
SG A:CYS176 2.2 27.4 1.0
SG A:CYS157 2.6 41.0 1.0
CB A:CYS179 2.7 25.0 1.0
CB A:CYS154 3.3 36.4 1.0
CB A:CYS176 3.3 28.1 1.0
N A:CYS176 3.6 29.6 1.0
CB A:CYS157 3.7 35.3 1.0
N A:CYS157 3.8 41.9 1.0
N A:CYS179 3.9 24.7 1.0
CA A:CYS179 3.9 28.8 1.0
CA A:CYS176 4.0 30.4 1.0
CA A:CYS157 4.3 42.8 1.0
CB A:ASN156 4.5 37.7 1.0
C A:CYS176 4.6 32.3 1.0
CA A:CYS154 4.7 38.4 1.0
C A:LEU175 4.7 29.8 1.0
O A:CYS176 4.7 27.8 1.0
O C:HOH271 4.7 31.6 1.0
C A:ASN156 4.8 42.0 1.0
ND2 A:ASN156 4.8 42.4 1.0
CG2 A:THR159 4.9 38.0 1.0
CA A:LEU175 4.9 31.4 1.0
CB A:LEU175 4.9 28.6 1.0
N A:ASN156 4.9 36.9 1.0
CA A:ASN156 5.0 35.2 1.0

Reference:

X.Yan, X.Yuan, J.Lv, B.Zhang, Y.Huang, Q.Li, J.Ma, Y.Li, X.Wang, Y.Li, Y.Yu, Q.Liu, T.Liu, W.Mi, C.Dong. Molecular Basis of SAP05-Mediated Ubiquitin-Independent Proteasomal Degradation of Transcription Factors Nat Commun V. 15 1170 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-45521-7
Page generated: Thu Oct 31 08:03:26 2024

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