Zinc in PDB 7z5h: Human Zn Matcap

Protein crystallography data

The structure of Human Zn Matcap, PDB code: 7z5h was solved by J.Bak, A.Adamopoulos, T.Heidebrecht, A.Perrakis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.08 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.646, 88.067, 165.581, 90, 90.77, 90
R / Rfree (%) 23.2 / 25.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Zn Matcap (pdb code 7z5h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Zn Matcap, PDB code: 7z5h:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 7z5h

Go back to Zinc Binding Sites List in 7z5h
Zinc binding site 1 out of 4 in the Human Zn Matcap


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Zn Matcap within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:46.2
occ:1.00
HE2 A:HIS280 1.3 30.0 0.0
HE2 A:HIS285 1.5 30.0 0.0
NE2 A:HIS280 2.2 44.4 1.0
OE1 A:GLU316 2.2 48.6 1.0
NE2 A:HIS285 2.3 41.8 1.0
OE2 A:GLU316 2.8 49.1 1.0
CD A:GLU316 2.9 48.3 1.0
CD2 A:HIS285 3.1 42.6 1.0
CE1 A:HIS280 3.2 43.1 1.0
CD2 A:HIS280 3.2 45.0 1.0
HD2 A:HIS285 3.2 42.6 1.0
HE1 A:TYR393 3.3 41.2 1.0
HH A:TYR393 3.3 30.0 0.0
HD2 A:HIS280 3.3 45.4 1.0
HE1 A:HIS280 3.3 42.4 1.0
CE1 A:HIS285 3.4 42.1 1.0
HE1 A:HIS285 3.6 41.4 1.0
OE2 A:GLU281 3.7 48.6 1.0
OH A:TYR393 4.1 45.9 1.0
CE1 A:TYR393 4.1 40.9 1.0
HB3 A:ALA319 4.2 44.5 1.0
ND1 A:HIS280 4.3 41.4 1.0
CG A:HIS285 4.3 42.3 1.0
CG A:HIS280 4.3 43.4 1.0
CG A:GLU316 4.3 47.0 1.0
HB2 A:ALA319 4.4 45.1 1.0
ND1 A:HIS285 4.4 41.9 1.0
CD A:GLU281 4.4 49.7 1.0
HA A:GLU316 4.5 46.0 1.0
OE1 A:GLU281 4.6 51.8 1.0
CB A:ALA319 4.6 44.9 1.0
CZ A:TYR393 4.6 42.0 1.0
HB3 A:GLU316 4.7 45.4 1.0
HG3 A:GLU316 4.8 47.2 1.0
HG2 A:GLU316 4.8 47.7 1.0
HB1 A:ALA319 4.8 45.3 1.0
CB A:GLU316 5.0 45.8 1.0

Zinc binding site 2 out of 4 in 7z5h

Go back to Zinc Binding Sites List in 7z5h
Zinc binding site 2 out of 4 in the Human Zn Matcap


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Zn Matcap within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:55.0
occ:1.00
HE2 B:HIS280 1.4 30.0 0.0
HE2 B:HIS285 1.5 30.0 0.0
NE2 B:HIS280 2.3 52.9 1.0
NE2 B:HIS285 2.3 52.7 1.0
OE1 B:GLU316 2.4 56.5 1.0
OE2 B:GLU316 2.8 58.0 1.0
CD B:GLU316 2.9 57.0 1.0
CD2 B:HIS285 3.1 53.4 1.0
HD2 B:HIS285 3.1 53.7 1.0
CD2 B:HIS280 3.2 53.1 1.0
CE1 B:HIS280 3.3 53.3 1.0
HH B:TYR393 3.3 30.0 0.0
HD2 B:HIS280 3.3 53.5 1.0
HE1 B:TYR393 3.4 53.4 1.0
CE1 B:HIS285 3.4 53.2 1.0
HE1 B:HIS280 3.4 53.2 1.0
OE2 B:GLU281 3.6 59.2 1.0
HE1 B:HIS285 3.7 52.8 1.0
OH B:TYR393 4.1 55.1 1.0
CE1 B:TYR393 4.2 53.7 1.0
CG B:HIS285 4.3 53.0 1.0
HB3 B:ALA319 4.3 55.5 1.0
CD B:GLU281 4.3 58.4 1.0
ND1 B:HIS280 4.4 53.5 1.0
CG B:HIS280 4.4 53.8 1.0
ND1 B:HIS285 4.4 53.1 1.0
HB2 B:ALA319 4.5 55.7 1.0
CG B:GLU316 4.5 56.4 1.0
OE1 B:GLU281 4.5 58.0 1.0
HA B:GLU316 4.6 54.2 1.0
CZ B:TYR393 4.7 54.4 1.0
CB B:ALA319 4.8 55.5 1.0
HG3 B:GLU316 4.9 56.8 1.0
HB3 B:GLU316 4.9 55.7 1.0
HG2 B:GLU316 4.9 56.3 1.0
HB1 B:ALA319 4.9 55.3 1.0

Zinc binding site 3 out of 4 in 7z5h

Go back to Zinc Binding Sites List in 7z5h
Zinc binding site 3 out of 4 in the Human Zn Matcap


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Zn Matcap within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn501

b:57.6
occ:1.00
HE2 C:HIS285 1.7 30.0 0.0
HE2 C:HIS280 1.7 30.0 0.0
NE2 C:HIS285 2.5 44.9 1.0
NE2 C:HIS280 2.5 49.7 1.0
OE1 C:GLU316 2.5 53.8 1.0
OE2 C:GLU316 2.8 57.0 1.0
CD C:GLU316 3.0 53.5 1.0
HD2 C:HIS285 3.2 45.6 1.0
CD2 C:HIS285 3.2 45.4 1.0
HH C:TYR393 3.3 30.0 0.0
CD2 C:HIS280 3.4 49.5 1.0
HE1 C:TYR393 3.4 46.5 1.0
HD2 C:HIS280 3.5 49.9 1.0
CE1 C:HIS280 3.5 49.3 1.0
OE2 C:GLU281 3.5 52.4 1.0
CE1 C:HIS285 3.6 45.0 1.0
HE1 C:HIS280 3.7 48.8 1.0
HE1 C:HIS285 3.8 44.4 1.0
OH C:TYR393 4.1 48.5 1.0
CD C:GLU281 4.3 53.2 1.0
CE1 C:TYR393 4.3 46.4 1.0
OE1 C:GLU281 4.3 57.4 1.0
CG C:HIS285 4.4 44.9 1.0
CG C:GLU316 4.5 52.0 1.0
ND1 C:HIS285 4.6 44.7 1.0
CG C:HIS280 4.6 49.0 1.0
HB3 C:ALA319 4.6 48.6 1.0
ND1 C:HIS280 4.6 48.7 1.0
HB2 C:ALA319 4.7 49.2 1.0
CZ C:TYR393 4.7 46.5 1.0
HA C:GLU316 4.8 51.5 1.0
HG3 C:GLU316 4.9 52.1 1.0
HG2 C:GLU316 5.0 52.3 1.0
HB3 C:GLU316 5.0 51.6 1.0

Zinc binding site 4 out of 4 in 7z5h

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Zinc binding site 4 out of 4 in the Human Zn Matcap


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Zn Matcap within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn501

b:44.8
occ:1.00
HE2 D:HIS285 1.4 30.0 0.0
HE2 D:HIS280 1.4 30.0 0.0
NE2 D:HIS285 2.2 38.2 1.0
OE1 D:GLU316 2.3 47.3 1.0
NE2 D:HIS280 2.3 36.8 1.0
OE2 D:GLU316 2.7 50.0 1.0
CD D:GLU316 2.8 46.6 1.0
CD2 D:HIS285 3.0 38.3 1.0
HD2 D:HIS285 3.1 38.2 1.0
CD2 D:HIS280 3.2 37.2 1.0
CE1 D:HIS280 3.3 35.8 1.0
CE1 D:HIS285 3.3 38.4 1.0
HD2 D:HIS280 3.3 37.8 1.0
HE1 D:TYR393 3.4 30.1 1.0
HH D:TYR393 3.4 30.0 0.0
HE1 D:HIS280 3.5 35.3 1.0
HE1 D:HIS285 3.6 37.6 1.0
OE2 D:GLU281 3.7 46.5 1.0
OH D:TYR393 4.2 31.8 1.0
CE1 D:TYR393 4.2 29.6 1.0
CG D:HIS285 4.2 36.9 1.0
HB3 D:ALA319 4.3 37.0 1.0
ND1 D:HIS285 4.3 38.0 1.0
CG D:GLU316 4.4 44.4 1.0
CD D:GLU281 4.4 46.1 1.0
CG D:HIS280 4.4 36.8 1.0
ND1 D:HIS280 4.4 35.2 1.0
HB2 D:ALA319 4.4 37.7 1.0
OE1 D:GLU281 4.5 48.9 1.0
HA D:GLU316 4.5 41.0 1.0
CB D:ALA319 4.7 37.5 1.0
CZ D:TYR393 4.7 30.1 1.0
HG3 D:GLU316 4.8 44.4 1.0
HG2 D:GLU316 4.8 44.9 1.0
HB3 D:GLU316 4.8 42.0 1.0
O D:HOH616 4.8 45.4 1.0
HB1 D:ALA319 4.8 37.9 1.0

Reference:

L.Landskron, J.Bak, A.Adamopoulos, K.Kaplani, M.Moraiti, L.G.Van Den Hengel, J.Y.Song, O.B.Bleijerveld, J.Nieuwenhuis, T.Heidebrecht, L.Henneman, M.J.Moutin, M.Barisic, S.Taraviras, A.Perrakis, T.R.Brummelkamp. Posttranslational Modification of Microtubules By the Matcap Detyrosinase. Science V. 376 N6020 2022.
ISSN: ESSN 1095-9203
PubMed: 35482892
DOI: 10.1126/SCIENCE.ABN6020
Page generated: Wed Oct 30 16:14:06 2024

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