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Zinc in PDB 7zmr: Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011

Enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011:
3.6.4.12;

Protein crystallography data

The structure of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011, PDB code: 7zmr was solved by M.Ye, M.Makola, J.A.Newman, M.Fairhead, E.Maclean, T.Krojer, H.Aitkenhead, C.Bountra, O.Gileadi, F.Von Delft, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 99.49 / 3.30
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 114.89, 198.954, 172.926, 90, 90, 90
R / Rfree (%) 24.3 / 29.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011 (pdb code 7zmr). 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 Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011, PDB code: 7zmr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7zmr

Go back to Zinc Binding Sites List in 7zmr
Zinc binding site 1 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011


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 Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:59.4
occ:1.00
SG A:CYS434 2.2 60.9 1.0
SG A:CYS427 2.3 80.4 1.0
SG A:CYS431 2.4 48.5 1.0
SG A:CYS411 2.7 65.0 1.0
CB A:CYS431 3.2 50.7 1.0
CB A:CYS427 3.2 69.1 1.0
CB A:CYS434 3.3 67.8 1.0
CB A:CYS411 3.4 66.7 1.0
N A:CYS431 3.8 51.7 1.0
CA A:CYS411 3.9 67.5 1.0
CA A:CYS431 4.1 51.4 1.0
N A:ARG412 4.1 66.3 1.0
CD2 A:HIS413 4.1 61.6 1.0
N A:CYS434 4.3 68.4 1.0
C A:GLY430 4.4 54.2 1.0
CA A:CYS434 4.4 70.0 1.0
C A:CYS411 4.4 68.0 1.0
CA A:CYS427 4.6 69.0 1.0
N A:GLY430 4.6 66.6 1.0
O A:CYS431 4.6 51.9 1.0
N A:HIS413 4.7 58.5 1.0
O A:CYS427 4.7 65.9 1.0
C A:CYS431 4.7 50.1 1.0
C A:CYS427 4.8 67.7 1.0
O A:GLY430 4.9 50.6 1.0
CB A:HIS413 4.9 63.6 1.0
CG A:HIS413 4.9 63.8 1.0
CA A:GLY430 4.9 57.9 1.0

Zinc binding site 2 out of 2 in 7zmr

Go back to Zinc Binding Sites List in 7zmr
Zinc binding site 2 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011


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 Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-011 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:63.0
occ:1.00
SG B:CYS434 2.1 63.1 1.0
SG B:CYS427 2.3 66.5 1.0
SG B:CYS411 2.4 71.4 1.0
SG B:CYS431 2.6 56.3 1.0
CB B:CYS411 3.2 71.0 1.0
CB B:CYS427 3.2 67.0 1.0
CB B:CYS434 3.3 67.7 1.0
CB B:CYS431 3.4 57.9 1.0
CA B:CYS411 3.7 68.6 1.0
N B:ARG412 4.1 65.2 1.0
N B:CYS431 4.1 57.5 1.0
CD2 B:HIS413 4.3 72.8 1.0
C B:CYS411 4.3 65.1 1.0
CA B:CYS431 4.3 57.1 1.0
N B:CYS434 4.3 64.9 1.0
O B:CYS427 4.4 62.7 1.0
CA B:CYS434 4.4 72.1 1.0
CA B:CYS427 4.5 70.0 1.0
N B:HIS413 4.6 62.4 1.0
C B:GLY430 4.6 59.4 1.0
C B:CYS427 4.7 66.9 1.0
O B:CYS431 4.8 53.3 1.0
CB B:HIS413 4.9 67.0 1.0
N B:GLY430 4.9 68.3 1.0
CG B:HIS413 4.9 70.3 1.0
C B:CYS431 4.9 56.3 1.0
N B:CYS411 5.0 70.3 1.0

Reference:

M.Ye, M.Makola, J.A.Newman, M.Fairhead, E.Maclean, T.Krojer, N.D.Wright, L.Koekemoer, A.Thompson, G.A.Bezerra, G.Yi, H.Li, V.L.Rangel, D.Mamalis, H.Aitkenhead, R.J.C.Gilbert, K.Duerr, B.G.Davis, C.Bountra, O.Gileadi, F.Von Delft. Gluebodies Improve Crystal Reliability and Diversity Through Transferable Nanobody Mutations That Introduce Constitutive Crystal Contacts To Be Published.
Page generated: Wed Oct 30 17:11:32 2024

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