Zinc in PDB 9gle: Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S

Enzymatic activity of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S

All present enzymatic activity of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S:
1.14.11.66; 1.14.11.69;

Protein crystallography data

The structure of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S, PDB code: 9gle was solved by M.Fairhead, C.Strain-Damerell, M.Ye, S.R.Mackinnon, D.Pinkas, E.M.Maclean, L.Koekemoer, D.Damerell, T.Krojer, C.H.Arrowsmith, A.Edwards, C.Bountra, W.Yue, N.Burgess-Brown, B.Marsden, F.Von Delft, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.45 / 1.88
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 117.7, 90.78, 90.67, 90, 107.19, 90
R / Rfree (%) 18.5 / 22.2

Other elements in 9gle:

The structure of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S also contains other interesting chemical elements:

Nickel (Ni) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S (pdb code 9gle). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S, PDB code: 9gle:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 9gle

Go back to Zinc Binding Sites List in 9gle
Zinc binding site 1 out of 2 in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:38.9
occ:1.00
SG A:CYS307 2.1 41.2 1.0
NE2 A:HIS241 2.1 37.6 1.0
SG A:CYS235 2.2 40.0 1.0
SG A:CYS309 2.4 41.6 1.0
H A:CYS309 2.9 68.1 1.0
CD2 A:HIS241 3.1 32.2 1.0
HB2 A:CYS235 3.1 42.7 1.0
CE1 A:HIS241 3.1 37.5 1.0
HD2 A:HIS241 3.2 33.7 1.0
CB A:CYS235 3.2 42.8 1.0
CB A:CYS307 3.3 45.8 1.0
HE1 A:HIS241 3.3 37.6 1.0
HB2 A:CYS307 3.3 43.7 1.0
HB3 A:CYS309 3.4 56.6 1.0
CB A:CYS309 3.5 61.4 1.0
HA A:CYS307 3.5 43.7 1.0
HB3 A:CYS235 3.6 42.7 1.0
H A:SER308 3.7 62.0 1.0
N A:CYS309 3.7 67.5 1.0
HG3 A:ARG310 3.8 69.2 1.0
CA A:CYS307 3.8 40.9 1.0
HA A:PHE238 3.9 32.8 1.0
H A:ARG310 4.0 57.6 1.0
CA A:CYS309 4.0 59.8 1.0
N A:SER308 4.1 62.7 1.0
HB3 A:CYS307 4.1 43.9 1.0
C A:CYS307 4.2 55.1 1.0
CG A:HIS241 4.2 33.6 1.0
ND1 A:HIS241 4.2 37.6 1.0
HD2 A:ARG310 4.3 69.2 1.0
HB2 A:CYS309 4.3 56.6 1.0
N A:ARG310 4.4 55.2 1.0
C A:CYS309 4.5 60.2 1.0
H A:ALA237 4.6 43.5 1.0
CA A:CYS235 4.6 44.5 1.0
CG A:ARG310 4.6 68.0 1.0
HA A:CYS235 4.7 44.6 1.0
O A:ALA237 4.7 33.2 1.0
HB2 A:ARG310 4.7 67.4 1.0
C A:SER308 4.8 79.6 1.0
CA A:PHE238 4.8 32.6 1.0
CD A:ARG310 4.8 71.9 1.0
O A:HOH552 4.9 48.6 1.0
HE A:ARG310 4.9 67.9 1.0
HA A:CYS309 5.0 61.7 1.0
C A:ALA237 5.0 31.2 1.0
O A:CYS307 5.0 49.0 1.0

Zinc binding site 2 out of 2 in 9gle

Go back to Zinc Binding Sites List in 9gle
Zinc binding site 2 out of 2 in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn404

b:39.9
occ:1.00
SG B:CYS307 2.0 39.9 1.0
NE2 B:HIS241 2.1 33.1 1.0
SG B:CYS235 2.3 41.5 1.0
SG B:CYS309 2.4 44.2 1.0
H B:CYS309 2.9 64.9 1.0
CD2 B:HIS241 3.0 33.6 1.0
HB2 B:CYS235 3.1 48.6 1.0
HD2 B:HIS241 3.2 33.6 1.0
CE1 B:HIS241 3.2 40.3 1.0
CB B:CYS307 3.2 42.1 1.0
CB B:CYS235 3.2 47.3 1.0
HB2 B:CYS307 3.3 42.7 1.0
HE1 B:HIS241 3.4 36.9 1.0
HB3 B:CYS309 3.4 56.5 1.0
CB B:CYS309 3.5 61.7 1.0
HB3 B:CYS235 3.5 48.6 1.0
HA B:CYS307 3.6 46.4 1.0
N B:CYS309 3.7 62.2 1.0
HG3 B:ARG310 3.7 56.2 1.0
H B:SER308 3.8 58.8 1.0
HA B:PHE238 3.9 34.8 1.0
CA B:CYS307 3.9 46.5 1.0
H B:ARG310 4.0 58.9 1.0
CA B:CYS309 4.0 55.4 1.0
HB3 B:CYS307 4.0 42.8 1.0
N B:SER308 4.1 59.7 1.0
CG B:HIS241 4.2 33.7 1.0
ND1 B:HIS241 4.2 33.5 1.0
C B:CYS307 4.2 47.7 1.0
HB2 B:CYS309 4.3 56.4 1.0
N B:ARG310 4.4 57.8 1.0
C B:CYS309 4.4 57.1 1.0
HD2 B:ARG310 4.6 59.1 1.0
CG B:ARG310 4.6 55.5 1.0
H B:ALA237 4.6 52.7 1.0
CA B:CYS235 4.6 58.9 1.0
HA B:CYS235 4.7 54.1 1.0
O B:HOH559 4.7 48.4 1.0
O B:ALA237 4.7 36.2 1.0
HB2 B:ARG310 4.7 57.7 1.0
C B:SER308 4.8 83.5 1.0
CA B:PHE238 4.8 37.6 1.0
HE B:ARG310 4.9 64.1 1.0
HA B:CYS309 4.9 58.4 1.0
HG3 B:MET313 4.9 63.2 1.0
CD B:ARG310 5.0 57.9 1.0
C B:ALA237 5.0 38.7 1.0

Reference:

M.Fairhead, C.Strain-Damerell, M.Ye, S.R.Mackinnon, D.Pinkas, E.M.Maclean, L.Koekemoer, D.Damerell, T.Krojer, W.Yue, N.Burgess-Brown, B.Marsden, F.Von Delft. A Fast, Parallel Method For Efficiently Exploring Crystallization Behaviour of Large Numbers of Protein Variants To Be Published.
Page generated: Thu Oct 31 15:38:41 2024

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