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Zinc in PDB 4xvu: Structure of GET3 Bound to the Transmembrane Domain of NYV1

Protein crystallography data

The structure of Structure of GET3 Bound to the Transmembrane Domain of NYV1, PDB code: 4xvu was solved by A.Mateja, M.Paduch, H.-Y.Chang, A.Szydlowska, A.A.Kossiakoff, R.S.Hegde, R.J.Keenan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.38 / 2.35
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 79.440, 109.230, 111.350, 63.05, 77.74, 70.17
R / Rfree (%) 19.7 / 23.4

Other elements in 4xvu:

The structure of Structure of GET3 Bound to the Transmembrane Domain of NYV1 also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of GET3 Bound to the Transmembrane Domain of NYV1 (pdb code 4xvu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of GET3 Bound to the Transmembrane Domain of NYV1, PDB code: 4xvu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4xvu

Go back to Zinc Binding Sites List in 4xvu
Zinc binding site 1 out of 2 in the Structure of GET3 Bound to the Transmembrane Domain of NYV1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of GET3 Bound to the Transmembrane Domain of NYV1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:55.8
occ:1.00
SG A:CYS285 2.3 73.4 1.0
SG A:CYS288 2.3 45.9 1.0
SG B:CYS285 2.3 80.6 1.0
SG B:CYS288 2.4 47.2 1.0
HB2 B:CYS288 2.9 68.5 1.0
HB2 A:CYS288 2.9 57.6 1.0
HB3 A:CYS285 3.1 91.2 1.0
CB A:CYS285 3.2 76.0 1.0
CB B:CYS288 3.2 57.1 1.0
CB A:CYS288 3.2 48.0 1.0
CB B:CYS285 3.2 85.9 1.0
HB2 B:CYS285 3.3 0.1 1.0
HB3 B:CYS285 3.3 0.1 1.0
HB2 A:CYS285 3.3 91.2 1.0
H A:CYS288 3.7 60.8 1.0
H B:CYS288 3.8 69.5 1.0
HB3 B:CYS288 3.8 68.5 1.0
HB3 A:CYS288 3.9 57.6 1.0
HH21 A:ARG287 4.0 80.6 1.0
HH21 B:ARG287 4.2 73.7 1.0
N A:CYS288 4.3 50.7 1.0
CA A:CYS288 4.3 48.1 1.0
CA B:CYS288 4.3 56.0 1.0
N B:CYS288 4.4 57.9 1.0
O B:HOH578 4.4 42.0 1.0
HA A:CYS288 4.6 57.8 1.0
NH2 A:ARG287 4.6 67.2 1.0
CA A:CYS285 4.6 72.0 1.0
O B:HOH565 4.6 62.6 1.0
HE A:ARG287 4.6 73.6 1.0
HA B:CYS288 4.6 67.2 1.0
HB3 A:ARG287 4.7 68.5 1.0
HB3 B:ARG287 4.7 71.2 1.0
CA B:CYS285 4.7 91.1 1.0
HE B:ARG287 4.7 69.0 1.0
NH2 B:ARG287 4.9 61.4 1.0
HA A:CYS285 4.9 86.4 1.0
HA B:CYS285 4.9 0.3 1.0
HH22 A:ARG287 5.0 80.6 1.0

Zinc binding site 2 out of 2 in 4xvu

Go back to Zinc Binding Sites List in 4xvu
Zinc binding site 2 out of 2 in the Structure of GET3 Bound to the Transmembrane Domain of NYV1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of GET3 Bound to the Transmembrane Domain of NYV1 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn403

b:56.2
occ:1.00
SG H:CYS288 2.3 41.5 1.0
SG G:CYS285 2.3 0.0 1.0
SG H:CYS285 2.3 58.0 1.0
SG G:CYS288 2.4 46.9 1.0
HB2 G:CYS288 2.8 58.1 1.0
CB G:CYS288 3.2 48.4 1.0
CB H:CYS285 3.2 60.2 1.0
HB3 H:CYS285 3.2 72.3 1.0
HB2 H:CYS285 3.2 72.3 1.0
HB2 H:CYS288 3.2 52.1 1.0
CB G:CYS285 3.4 0.2 1.0
HB3 G:CYS285 3.4 0.7 1.0
CB H:CYS288 3.4 43.5 1.0
HB2 G:CYS285 3.5 0.7 1.0
H G:CYS288 3.6 62.6 1.0
HB3 G:CYS288 3.8 58.1 1.0
O G:HOH585 3.9 54.7 1.0
H H:CYS288 4.0 52.2 1.0
HB3 H:CYS288 4.0 52.1 1.0
O G:HOH553 4.2 42.4 1.0
N G:CYS288 4.2 52.2 1.0
CA G:CYS288 4.2 49.1 1.0
CA H:CYS288 4.5 42.5 1.0
N H:CYS288 4.5 43.5 1.0
HA G:CYS288 4.5 58.9 1.0
HB3 G:ARG287 4.6 68.9 1.0
CA H:CYS285 4.7 0.6 1.0
HA H:CYS288 4.7 51.0 1.0
HE G:ARG287 4.7 72.0 1.0
O H:HOH564 4.8 65.3 1.0
CA G:CYS285 4.8 0.8 1.0
HB3 H:ARG287 4.8 56.5 1.0
HH21 H:ARG287 4.8 62.4 1.0
HH21 G:ARG287 4.9 77.1 1.0
HA H:CYS285 4.9 0.7 1.0
O G:HOH579 5.0 51.4 1.0

Reference:

A.Mateja, M.Paduch, H.Y.Chang, A.Szydlowska, A.A.Kossiakoff, R.S.Hegde, R.J.Keenan. Protein Targeting. Structure of the GET3 Targeting Factor in Complex with Its Membrane Protein Cargo. Science V. 347 1152 2015.
ISSN: ESSN 1095-9203
PubMed: 25745174
DOI: 10.1126/SCIENCE.1261671
Page generated: Sun Oct 27 10:49:44 2024

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