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Zinc in PDB 5jh9: Crystal Structure of PRAPE1

Enzymatic activity of Crystal Structure of PRAPE1

All present enzymatic activity of Crystal Structure of PRAPE1:
3.4.11.22;

Protein crystallography data

The structure of Crystal Structure of PRAPE1, PDB code: 5jh9 was solved by N.N.Noda, W.Adachi, F.Inagaki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.79 / 2.10
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 140.428, 140.428, 348.922, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 20.7

Other elements in 5jh9:

The structure of Crystal Structure of PRAPE1 also contains other interesting chemical elements:

Arsenic (As) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of PRAPE1 (pdb code 5jh9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Crystal Structure of PRAPE1, PDB code: 5jh9:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 5jh9

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Zinc binding site 1 out of 8 in the Crystal Structure of PRAPE1


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 PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:57.6
occ:1.00
O1 A:CAC603 2.0 30.6 1.0
OD1 A:ASP303 2.1 28.4 1.0
O A:HOH765 2.1 20.4 1.0
OD1 A:ASP385 2.2 29.1 1.0
OD2 A:ASP385 2.4 28.7 1.0
CG A:ASP385 2.7 29.0 1.0
NE2 A:HIS132 2.7 26.9 1.0
CG A:ASP303 3.0 28.2 1.0
OD2 A:ASP303 3.1 27.7 1.0
AS A:CAC603 3.3 31.7 1.0
ZN A:ZN602 3.5 32.8 1.0
CE1 A:HIS132 3.6 27.0 1.0
CD2 A:HIS132 3.7 27.1 1.0
C2 A:CAC603 3.7 31.1 1.0
OE1 A:GLU339 3.9 29.6 1.0
O2 A:CAC603 4.0 30.1 1.0
CG2 A:VAL386 4.0 29.2 1.0
OE2 A:GLU339 4.1 29.8 1.0
CB A:ASP304 4.1 29.6 1.0
OE2 A:GLU340 4.2 30.2 1.0
CB A:ASP385 4.2 28.9 1.0
CD A:GLU339 4.2 29.4 1.0
CB A:ASP303 4.4 28.2 1.0
O A:VAL386 4.5 29.0 1.0
N A:VAL386 4.6 29.1 1.0
CG A:ASP304 4.7 30.2 1.0
CD A:GLU340 4.8 29.9 1.0
ND1 A:HIS132 4.8 27.2 1.0
CA A:ASP303 4.8 28.6 1.0
CG A:HIS132 4.8 27.3 1.0
SD A:MET478 4.9 26.5 1.0
C A:ASP303 4.9 28.5 1.0
CA A:ASP385 4.9 29.0 1.0
C1 A:CAC603 4.9 30.5 1.0
OE1 A:GLU340 5.0 29.6 1.0
O A:HOH822 5.0 28.2 1.0
CA A:ASP304 5.0 29.5 1.0

Zinc binding site 2 out of 8 in 5jh9

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Zinc binding site 2 out of 8 in the Crystal Structure of PRAPE1


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 PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:32.8
occ:1.00
OD2 A:ASP303 2.0 27.7 1.0
O2 A:CAC603 2.2 30.1 1.0
OE2 A:GLU340 2.2 30.2 1.0
NE2 A:HIS479 2.3 27.8 1.0
OE1 A:GLU340 2.4 29.6 1.0
O1 A:CAC603 2.6 30.6 1.0
CD A:GLU340 2.6 29.9 1.0
AS A:CAC603 2.9 31.7 1.0
CG A:ASP303 2.9 28.2 1.0
CD2 A:HIS479 3.1 27.7 1.0
CE1 A:HIS479 3.4 28.2 1.0
OD1 A:ASP303 3.4 28.4 1.0
ZN A:ZN601 3.5 57.6 1.0
O A:HOH765 4.0 20.4 1.0
C1 A:CAC603 4.0 30.5 1.0
NE2 B:HIS210 4.0 30.4 1.0
CB A:ASP303 4.1 28.2 1.0
CG A:GLU340 4.2 29.6 1.0
O A:HOH760 4.2 23.9 1.0
CG A:HIS479 4.3 27.8 1.0
CE1 B:HIS210 4.3 29.9 1.0
ND1 A:HIS479 4.4 28.3 1.0
SD A:MET478 4.4 26.5 1.0
OE1 A:GLU339 4.5 29.6 1.0
O A:HOH740 4.5 29.6 1.0
CG A:MET478 4.5 26.5 1.0
C2 A:CAC603 4.5 31.1 1.0
NE2 A:HIS132 4.8 26.9 1.0
CD1 A:LEU136 4.9 26.6 1.0
CE1 A:HIS132 4.9 27.0 1.0

Zinc binding site 3 out of 8 in 5jh9

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Zinc binding site 3 out of 8 in the Crystal Structure of PRAPE1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn601

b:61.4
occ:1.00
O1 B:CAC603 1.9 28.1 1.0
O B:HOH852 2.0 24.6 1.0
OD1 B:ASP303 2.1 27.7 1.0
OD1 B:ASP385 2.4 29.1 1.0
OD2 B:ASP385 2.5 29.0 1.0
NE2 B:HIS132 2.7 31.1 1.0
CG B:ASP385 2.8 28.9 1.0
CG B:ASP303 3.0 27.6 1.0
AS B:CAC603 3.1 30.7 1.0
OD2 B:ASP303 3.2 27.2 1.0
ZN B:ZN602 3.4 32.9 1.0
C2 B:CAC603 3.6 29.3 1.0
CD2 B:HIS132 3.7 31.2 1.0
CE1 B:HIS132 3.7 31.0 1.0
O2 B:CAC603 3.8 29.1 1.0
OE1 B:GLU339 3.9 26.6 1.0
OE2 B:GLU339 4.0 26.2 1.0
OE2 B:GLU340 4.1 27.5 1.0
CD B:GLU339 4.2 26.4 1.0
CG2 B:VAL386 4.2 29.1 1.0
CB B:ASP304 4.2 28.2 1.0
CB B:ASP385 4.3 28.6 1.0
CB B:ASP303 4.4 27.7 1.0
O B:VAL386 4.6 28.1 1.0
CD B:GLU340 4.8 27.6 1.0
N B:VAL386 4.8 28.8 1.0
CG B:ASP304 4.8 28.4 1.0
C1 B:CAC603 4.8 29.6 1.0
ND1 B:HIS132 4.8 31.1 1.0
CA B:ASP303 4.8 27.9 1.0
CG B:HIS132 4.9 31.2 1.0
SD B:MET478 4.9 25.5 1.0
C B:ASP303 4.9 28.0 1.0
O B:HOH845 5.0 26.1 1.0

Zinc binding site 4 out of 8 in 5jh9

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Zinc binding site 4 out of 8 in the Crystal Structure of PRAPE1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:32.9
occ:1.00
O2 B:CAC603 2.0 29.1 1.0
OE2 B:GLU340 2.0 27.5 1.0
OD2 B:ASP303 2.0 27.2 1.0
NE2 B:HIS479 2.3 27.3 1.0
O1 B:CAC603 2.6 28.1 1.0
OE1 B:GLU340 2.6 27.6 1.0
CD B:GLU340 2.7 27.6 1.0
AS B:CAC603 2.8 30.7 1.0
CG B:ASP303 3.0 27.6 1.0
CD2 B:HIS479 3.1 27.1 1.0
OD1 B:ASP303 3.3 27.7 1.0
CE1 B:HIS479 3.4 27.6 1.0
ZN B:ZN601 3.4 61.4 1.0
O B:HOH852 3.8 24.6 1.0
C1 B:CAC603 3.9 29.6 1.0
NE2 A:HIS210 4.1 28.0 1.0
O B:HOH780 4.1 24.0 1.0
CG B:GLU340 4.2 27.8 1.0
CB B:ASP303 4.2 27.7 1.0
CG B:HIS479 4.3 27.3 1.0
CE1 A:HIS210 4.3 27.5 1.0
ND1 B:HIS479 4.4 27.7 1.0
SD B:MET478 4.4 25.5 1.0
OE1 B:GLU339 4.5 26.6 1.0
C2 B:CAC603 4.5 29.3 1.0
CG B:MET478 4.6 25.8 1.0
O B:HOH790 4.8 35.9 1.0
NE2 B:HIS132 4.8 31.1 1.0
CD1 B:LEU136 4.8 30.2 1.0
CE1 B:HIS132 4.9 31.0 1.0

Zinc binding site 5 out of 8 in 5jh9

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Zinc binding site 5 out of 8 in the Crystal Structure of PRAPE1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn601

b:56.0
occ:1.00
O C:HOH861 2.1 22.2 1.0
O1 C:CAC603 2.1 26.2 1.0
OD1 C:ASP303 2.2 24.6 1.0
OD1 C:ASP385 2.3 24.2 1.0
OD2 C:ASP385 2.3 24.1 1.0
CG C:ASP385 2.6 24.2 1.0
NE2 C:HIS132 2.7 24.6 1.0
CG C:ASP303 3.1 24.5 1.0
OD2 C:ASP303 3.3 24.4 1.0
AS C:CAC603 3.4 27.2 1.0
CD2 C:HIS132 3.6 24.2 1.0
ZN C:ZN602 3.6 29.8 1.0
CE1 C:HIS132 3.6 24.4 1.0
C2 C:CAC603 3.7 26.8 1.0
OE1 C:GLU339 3.9 24.3 1.0
CB C:ASP304 4.1 25.2 1.0
CG2 C:VAL386 4.1 24.3 1.0
CB C:ASP385 4.1 24.2 1.0
OE2 C:GLU340 4.1 25.3 1.0
O2 C:CAC603 4.1 24.6 1.0
OE2 C:GLU339 4.3 24.6 1.0
CD C:GLU339 4.3 24.3 1.0
CB C:ASP303 4.5 24.6 1.0
O C:VAL386 4.5 24.2 1.0
CG C:ASP304 4.6 25.5 1.0
N C:VAL386 4.6 24.3 1.0
ND1 C:HIS132 4.7 24.0 1.0
CG C:HIS132 4.8 23.9 1.0
CA C:ASP303 4.8 24.7 1.0
O C:HOH832 4.9 24.2 1.0
CD C:GLU340 4.9 25.0 1.0
CA C:ASP385 4.9 24.4 1.0
C C:ASP303 4.9 24.8 1.0
CA C:ASP304 4.9 25.3 1.0
N C:ASP304 4.9 25.0 1.0
OD2 C:ASP304 5.0 25.5 1.0
C1 C:CAC603 5.0 26.4 1.0

Zinc binding site 6 out of 8 in 5jh9

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Zinc binding site 6 out of 8 in the Crystal Structure of PRAPE1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn602

b:29.8
occ:1.00
OD2 C:ASP303 2.1 24.4 1.0
OE2 C:GLU340 2.1 25.3 1.0
NE2 C:HIS479 2.2 24.1 1.0
O2 C:CAC603 2.2 24.6 1.0
OE1 C:GLU340 2.5 24.8 1.0
O1 C:CAC603 2.5 26.2 1.0
CD C:GLU340 2.6 25.0 1.0
AS C:CAC603 2.9 27.2 1.0
CG C:ASP303 3.0 24.5 1.0
CD2 C:HIS479 3.1 24.1 1.0
CE1 C:HIS479 3.3 24.4 1.0
OD1 C:ASP303 3.4 24.6 1.0
ZN C:ZN601 3.6 56.0 1.0
O C:HOH861 3.8 22.2 1.0
C1 C:CAC603 4.0 26.4 1.0
O C:HOH754 4.0 21.8 1.0
CG C:GLU340 4.1 24.7 1.0
NE2 D:HIS210 4.1 27.6 1.0
CB C:ASP303 4.2 24.6 1.0
CG C:HIS479 4.3 24.2 1.0
ND1 C:HIS479 4.3 24.5 1.0
CE1 D:HIS210 4.4 27.0 1.0
OE1 C:GLU339 4.5 24.3 1.0
SD C:MET478 4.5 23.8 1.0
C2 C:CAC603 4.6 26.8 1.0
CG C:MET478 4.7 23.6 1.0
O C:HOH795 4.7 29.8 1.0
NE2 C:HIS132 4.7 24.6 1.0
CE1 C:HIS132 4.8 24.4 1.0
CD1 C:LEU136 4.9 25.1 1.0

Zinc binding site 7 out of 8 in 5jh9

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Zinc binding site 7 out of 8 in the Crystal Structure of PRAPE1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn601

b:54.8
occ:1.00
O1 D:CAC603 1.9 29.3 1.0
OD1 D:ASP303 2.0 26.8 1.0
O D:HOH829 2.2 23.9 1.0
OD2 D:ASP385 2.3 30.6 1.0
OD1 D:ASP385 2.4 29.4 1.0
NE2 D:HIS132 2.6 28.8 1.0
CG D:ASP385 2.7 29.9 1.0
CG D:ASP303 3.0 26.9 1.0
AS D:CAC603 3.2 31.2 1.0
OD2 D:ASP303 3.3 26.7 1.0
ZN D:ZN602 3.5 33.9 1.0
CD2 D:HIS132 3.6 28.2 1.0
CE1 D:HIS132 3.6 28.3 1.0
OE1 D:GLU339 3.8 26.5 1.0
C2 D:CAC603 3.8 30.2 1.0
O2 D:CAC603 3.9 29.3 1.0
OE2 D:GLU340 4.0 28.1 1.0
OE2 D:GLU339 4.0 26.7 1.0
CD D:GLU339 4.1 26.4 1.0
CB D:ASP304 4.1 27.2 1.0
CG2 D:VAL386 4.2 26.7 1.0
CB D:ASP385 4.2 29.7 1.0
CB D:ASP303 4.4 26.6 1.0
O D:VAL386 4.7 26.4 1.0
CD D:GLU340 4.7 27.7 1.0
CG D:ASP304 4.7 27.9 1.0
ND1 D:HIS132 4.7 27.5 1.0
CG D:HIS132 4.8 27.3 1.0
CA D:ASP303 4.8 26.6 1.0
N D:VAL386 4.8 26.5 1.0
OE1 D:GLU340 4.8 27.4 1.0
C1 D:CAC603 4.8 29.8 1.0
C D:ASP303 4.9 26.4 1.0
O D:HOH871 4.9 25.8 1.0
N D:ASP304 4.9 26.6 1.0
CA D:ASP304 5.0 27.0 1.0
SD D:MET478 5.0 25.8 1.0

Zinc binding site 8 out of 8 in 5jh9

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Zinc binding site 8 out of 8 in the Crystal Structure of PRAPE1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of PRAPE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn602

b:33.9
occ:1.00
OD2 D:ASP303 2.0 26.7 1.0
O2 D:CAC603 2.2 29.3 1.0
NE2 D:HIS479 2.2 26.9 1.0
OE2 D:GLU340 2.2 28.1 1.0
OE1 D:GLU340 2.4 27.4 1.0
O1 D:CAC603 2.6 29.3 1.0
CD D:GLU340 2.7 27.7 1.0
CG D:ASP303 2.9 26.9 1.0
AS D:CAC603 3.0 31.2 1.0
CD2 D:HIS479 3.1 26.6 1.0
CE1 D:HIS479 3.3 27.2 1.0
OD1 D:ASP303 3.3 26.8 1.0
ZN D:ZN601 3.5 54.8 1.0
O D:HOH829 3.9 23.9 1.0
C1 D:CAC603 4.0 29.8 1.0
O D:HOH742 4.1 22.9 1.0
NE2 C:HIS210 4.1 28.9 1.0
CB D:ASP303 4.1 26.6 1.0
CG D:GLU340 4.2 27.8 1.0
CG D:HIS479 4.3 26.8 1.0
ND1 D:HIS479 4.3 27.2 1.0
CE1 C:HIS210 4.4 28.3 1.0
OE1 D:GLU339 4.4 26.5 1.0
SD D:MET478 4.5 25.8 1.0
O D:HOH800 4.6 31.9 1.0
CG D:MET478 4.7 25.6 1.0
C2 D:CAC603 4.7 30.2 1.0
NE2 D:HIS132 4.8 28.8 1.0
CD1 D:LEU136 4.8 25.5 1.0
CE1 D:HIS132 4.9 28.3 1.0

Reference:

A.Yamasaki, Y.Watanabe, W.Adachi, K.Suzuki, K.Matoba, H.Kirisako, H.Kumeta, H.Nakatogawa, Y.Ohsumi, F.Inagaki, N.N.Noda. Structural Basis For Receptor-Mediated Selective Autophagy of Aminopeptidase I Aggregates Cell Rep V. 16 19 2016.
ISSN: ESSN 2211-1247
PubMed: 27320913
DOI: 10.1016/J.CELREP.2016.05.066
Page generated: Sun Oct 27 18:57:11 2024

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