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Zinc in PDB 6pev: Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase

Zinc Binding Sites:

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>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Zinc atom in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase (pdb code 6pev). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 24 binding sites of Zinc where determined in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase, PDB code: 6pev:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 24 in 6pev

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Zinc binding site 1 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1000

b:41.7
occ:1.00
ZN A:ZN1001 1.3 47.0 1.0
OD1 A:ASP324 2.1 21.7 1.0
OD1 A:ASP434 2.1 21.1 1.0
NE2 A:HIS86 2.2 19.1 1.0
OD2 A:ASP324 2.5 21.7 1.0
CG A:ASP324 2.5 21.7 1.0
CE1 A:HIS86 2.7 19.1 1.0
CG A:ASP434 3.0 21.1 1.0
OD2 A:ASP434 3.2 21.1 1.0
OE1 A:GLU379 3.4 20.6 1.0
CD2 A:HIS86 3.5 19.1 1.0
OE2 A:GLU380 3.7 19.9 1.0
CB A:ASP324 3.8 21.7 1.0
CB A:ASN325 3.8 20.8 1.0
C A:ASP324 3.9 21.7 1.0
O A:ASP324 3.9 21.7 1.0
ND1 A:HIS86 4.0 19.1 1.0
CD A:GLU379 4.1 20.6 1.0
CA A:ASP324 4.2 21.7 1.0
N A:ASN325 4.3 20.8 1.0
CG A:HIS86 4.3 19.1 1.0
CE A:MET533 4.4 21.0 1.0
CB A:ASP434 4.4 21.1 1.0
OE2 A:GLU379 4.5 20.6 1.0
NE2 A:HIS534 4.5 21.0 1.0
ND2 A:ASN325 4.6 20.8 1.0
CD A:GLU380 4.6 19.9 1.0
CA A:ASN325 4.7 20.8 1.0
CG A:ASN325 4.7 20.8 1.0
OE1 A:GLU380 4.8 19.9 1.0
N A:MET435 4.9 20.0 1.0

Zinc binding site 2 out of 24 in 6pev

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Zinc binding site 2 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:47.0
occ:1.00
ZN A:ZN1000 1.3 41.7 1.0
OD1 A:ASP434 2.2 21.1 1.0
OD2 A:ASP434 2.2 21.1 1.0
OD1 A:ASP324 2.4 21.7 1.0
CG A:ASP434 2.5 21.1 1.0
OD2 A:ASP324 2.9 21.7 1.0
NE2 A:HIS86 3.0 19.1 1.0
CG A:ASP324 3.0 21.7 1.0
OE1 A:GLU379 3.5 20.6 1.0
CE A:MET533 3.5 21.0 1.0
CE1 A:HIS86 3.8 19.1 1.0
OE2 A:GLU379 3.9 20.6 1.0
CD A:GLU379 3.9 20.6 1.0
CB A:ASP434 4.0 21.1 1.0
CD2 A:HIS86 4.1 19.1 1.0
NE2 A:HIS534 4.2 21.0 1.0
OE2 A:GLU380 4.5 19.9 1.0
CB A:ASP324 4.5 21.7 1.0
N A:MET435 4.7 20.0 1.0
CB A:ASN325 4.8 20.8 1.0
CA A:ASP434 4.9 21.1 1.0
C A:ASP324 4.9 21.7 1.0
CD2 A:HIS534 5.0 21.0 1.0
OE1 A:GLU380 5.0 19.9 1.0

Zinc binding site 3 out of 24 in 6pev

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Zinc binding site 3 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1000

b:41.7
occ:1.00
ZN B:ZN1001 1.3 47.0 1.0
OD1 B:ASP324 2.1 21.7 1.0
OD1 B:ASP434 2.1 21.1 1.0
NE2 B:HIS86 2.2 19.1 1.0
CG B:ASP324 2.5 21.7 1.0
OD2 B:ASP324 2.5 21.7 1.0
CE1 B:HIS86 2.7 19.1 1.0
CG B:ASP434 3.0 21.1 1.0
OD2 B:ASP434 3.2 21.1 1.0
OE1 B:GLU379 3.4 20.6 1.0
CD2 B:HIS86 3.5 19.1 1.0
OE2 B:GLU380 3.7 19.9 1.0
CB B:ASP324 3.8 21.7 1.0
CB B:ASN325 3.8 20.8 1.0
C B:ASP324 3.9 21.7 1.0
O B:ASP324 3.9 21.7 1.0
ND1 B:HIS86 4.0 19.1 1.0
CD B:GLU379 4.1 20.6 1.0
CA B:ASP324 4.2 21.7 1.0
N B:ASN325 4.3 20.8 1.0
CG B:HIS86 4.3 19.1 1.0
CE B:MET533 4.4 21.0 1.0
CB B:ASP434 4.4 21.1 1.0
OE2 B:GLU379 4.5 20.6 1.0
NE2 B:HIS534 4.5 21.0 1.0
ND2 B:ASN325 4.6 20.8 1.0
CD B:GLU380 4.6 19.9 1.0
CA B:ASN325 4.7 20.8 1.0
CG B:ASN325 4.7 20.8 1.0
OE1 B:GLU380 4.8 19.9 1.0
N B:MET435 4.9 20.0 1.0

Zinc binding site 4 out of 24 in 6pev

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Zinc binding site 4 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:47.0
occ:1.00
ZN B:ZN1000 1.3 41.7 1.0
OD1 B:ASP434 2.2 21.1 1.0
OD2 B:ASP434 2.2 21.1 1.0
OD1 B:ASP324 2.4 21.7 1.0
CG B:ASP434 2.5 21.1 1.0
OD2 B:ASP324 2.9 21.7 1.0
NE2 B:HIS86 3.0 19.1 1.0
CG B:ASP324 3.0 21.7 1.0
OE1 B:GLU379 3.5 20.6 1.0
CE B:MET533 3.5 21.0 1.0
CE1 B:HIS86 3.8 19.1 1.0
OE2 B:GLU379 3.9 20.6 1.0
CD B:GLU379 3.9 20.6 1.0
CB B:ASP434 4.0 21.1 1.0
CD2 B:HIS86 4.1 19.1 1.0
NE2 B:HIS534 4.2 21.0 1.0
OE2 B:GLU380 4.5 19.9 1.0
CB B:ASP324 4.5 21.7 1.0
N B:MET435 4.7 20.0 1.0
CB B:ASN325 4.8 20.8 1.0
CA B:ASP434 4.9 21.1 1.0
C B:ASP324 4.9 21.7 1.0
CD2 B:HIS534 5.0 21.0 1.0
OE1 B:GLU380 5.0 19.9 1.0

Zinc binding site 5 out of 24 in 6pev

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Zinc binding site 5 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1000

b:41.7
occ:1.00
ZN C:ZN1001 1.3 47.0 1.0
OD1 C:ASP324 2.1 21.7 1.0
OD1 C:ASP434 2.1 21.1 1.0
NE2 C:HIS86 2.2 19.1 1.0
OD2 C:ASP324 2.5 21.7 1.0
CG C:ASP324 2.5 21.7 1.0
CE1 C:HIS86 2.7 19.1 1.0
CG C:ASP434 3.0 21.1 1.0
OD2 C:ASP434 3.2 21.1 1.0
OE1 C:GLU379 3.4 20.6 1.0
CD2 C:HIS86 3.5 19.1 1.0
OE2 C:GLU380 3.7 19.9 1.0
CB C:ASP324 3.8 21.7 1.0
CB C:ASN325 3.8 20.8 1.0
C C:ASP324 3.9 21.7 1.0
O C:ASP324 3.9 21.7 1.0
ND1 C:HIS86 4.0 19.1 1.0
CD C:GLU379 4.1 20.6 1.0
CA C:ASP324 4.2 21.7 1.0
N C:ASN325 4.3 20.8 1.0
CG C:HIS86 4.4 19.1 1.0
CE C:MET533 4.4 21.0 1.0
CB C:ASP434 4.4 21.1 1.0
OE2 C:GLU379 4.5 20.6 1.0
NE2 C:HIS534 4.5 21.0 1.0
ND2 C:ASN325 4.6 20.8 1.0
CD C:GLU380 4.6 19.9 1.0
CA C:ASN325 4.7 20.8 1.0
CG C:ASN325 4.7 20.8 1.0
OE1 C:GLU380 4.8 19.9 1.0
N C:MET435 4.9 20.0 1.0

Zinc binding site 6 out of 24 in 6pev

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Zinc binding site 6 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1001

b:47.0
occ:1.00
ZN C:ZN1000 1.3 41.7 1.0
OD1 C:ASP434 2.2 21.1 1.0
OD2 C:ASP434 2.2 21.1 1.0
OD1 C:ASP324 2.4 21.7 1.0
CG C:ASP434 2.5 21.1 1.0
OD2 C:ASP324 2.9 21.7 1.0
NE2 C:HIS86 3.0 19.1 1.0
CG C:ASP324 3.0 21.7 1.0
OE1 C:GLU379 3.5 20.6 1.0
CE C:MET533 3.5 21.0 1.0
CE1 C:HIS86 3.8 19.1 1.0
OE2 C:GLU379 3.9 20.6 1.0
CD C:GLU379 3.9 20.6 1.0
CB C:ASP434 4.0 21.1 1.0
CD2 C:HIS86 4.1 19.1 1.0
NE2 C:HIS534 4.2 21.0 1.0
OE2 C:GLU380 4.5 19.9 1.0
CB C:ASP324 4.5 21.7 1.0
N C:MET435 4.7 20.0 1.0
CB C:ASN325 4.8 20.8 1.0
CA C:ASP434 4.9 21.1 1.0
C C:ASP324 4.9 21.7 1.0
CD2 C:HIS534 5.0 21.0 1.0
OE1 C:GLU380 5.0 19.9 1.0

Zinc binding site 7 out of 24 in 6pev

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Zinc binding site 7 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1000

b:41.7
occ:1.00
ZN D:ZN1001 1.3 47.0 1.0
OD1 D:ASP324 2.1 21.7 1.0
OD1 D:ASP434 2.1 21.1 1.0
NE2 D:HIS86 2.2 19.1 1.0
CG D:ASP324 2.5 21.7 1.0
OD2 D:ASP324 2.5 21.7 1.0
CE1 D:HIS86 2.7 19.1 1.0
CG D:ASP434 3.0 21.1 1.0
OD2 D:ASP434 3.2 21.1 1.0
OE1 D:GLU379 3.4 20.6 1.0
CD2 D:HIS86 3.5 19.1 1.0
OE2 D:GLU380 3.7 19.9 1.0
CB D:ASP324 3.8 21.7 1.0
CB D:ASN325 3.8 20.8 1.0
C D:ASP324 3.9 21.7 1.0
O D:ASP324 3.9 21.7 1.0
ND1 D:HIS86 4.0 19.1 1.0
CD D:GLU379 4.1 20.6 1.0
CA D:ASP324 4.2 21.7 1.0
N D:ASN325 4.3 20.8 1.0
CG D:HIS86 4.3 19.1 1.0
CE D:MET533 4.4 21.0 1.0
CB D:ASP434 4.4 21.1 1.0
OE2 D:GLU379 4.5 20.6 1.0
NE2 D:HIS534 4.5 21.0 1.0
ND2 D:ASN325 4.6 20.8 1.0
CD D:GLU380 4.6 19.9 1.0
CA D:ASN325 4.7 20.8 1.0
CG D:ASN325 4.7 20.8 1.0
OE1 D:GLU380 4.8 19.9 1.0
N D:MET435 4.9 20.0 1.0

Zinc binding site 8 out of 24 in 6pev

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Zinc binding site 8 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1001

b:47.0
occ:1.00
ZN D:ZN1000 1.3 41.7 1.0
OD1 D:ASP434 2.2 21.1 1.0
OD2 D:ASP434 2.2 21.1 1.0
OD1 D:ASP324 2.4 21.7 1.0
CG D:ASP434 2.5 21.1 1.0
OD2 D:ASP324 2.9 21.7 1.0
NE2 D:HIS86 3.0 19.1 1.0
CG D:ASP324 3.0 21.7 1.0
OE1 D:GLU379 3.5 20.6 1.0
CE D:MET533 3.5 21.0 1.0
CE1 D:HIS86 3.8 19.1 1.0
OE2 D:GLU379 3.9 20.6 1.0
CD D:GLU379 3.9 20.6 1.0
CB D:ASP434 4.0 21.1 1.0
CD2 D:HIS86 4.1 19.1 1.0
NE2 D:HIS534 4.2 21.0 1.0
OE2 D:GLU380 4.5 19.9 1.0
CB D:ASP324 4.5 21.7 1.0
N D:MET435 4.7 20.0 1.0
CB D:ASN325 4.8 20.8 1.0
CA D:ASP434 4.9 21.1 1.0
C D:ASP324 4.9 21.7 1.0
CD2 D:HIS534 5.0 21.0 1.0
OE1 D:GLU380 5.0 19.9 1.0

Zinc binding site 9 out of 24 in 6pev

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Zinc binding site 9 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn1000

b:41.7
occ:1.00
ZN E:ZN1001 1.3 47.0 1.0
OD1 E:ASP324 2.1 21.7 1.0
OD1 E:ASP434 2.1 21.1 1.0
NE2 E:HIS86 2.2 19.1 1.0
CG E:ASP324 2.5 21.7 1.0
OD2 E:ASP324 2.5 21.7 1.0
CE1 E:HIS86 2.7 19.1 1.0
CG E:ASP434 3.0 21.1 1.0
OD2 E:ASP434 3.2 21.1 1.0
OE1 E:GLU379 3.4 20.6 1.0
CD2 E:HIS86 3.5 19.1 1.0
OE2 E:GLU380 3.7 19.9 1.0
CB E:ASP324 3.8 21.7 1.0
CB E:ASN325 3.8 20.8 1.0
C E:ASP324 3.9 21.7 1.0
O E:ASP324 3.9 21.7 1.0
ND1 E:HIS86 4.0 19.1 1.0
CD E:GLU379 4.1 20.6 1.0
CA E:ASP324 4.2 21.7 1.0
N E:ASN325 4.3 20.8 1.0
CG E:HIS86 4.4 19.1 1.0
CE E:MET533 4.4 21.0 1.0
CB E:ASP434 4.4 21.1 1.0
OE2 E:GLU379 4.5 20.6 1.0
NE2 E:HIS534 4.5 21.0 1.0
ND2 E:ASN325 4.6 20.8 1.0
CD E:GLU380 4.6 19.9 1.0
CA E:ASN325 4.7 20.8 1.0
CG E:ASN325 4.7 20.8 1.0
OE1 E:GLU380 4.8 19.9 1.0
N E:MET435 4.9 20.0 1.0

Zinc binding site 10 out of 24 in 6pev

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Zinc binding site 10 out of 24 in the Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Cryoem Plasmodium Falciparum M18 Aspartyl Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn1001

b:47.0
occ:1.00
ZN E:ZN1000 1.3 41.7 1.0
OD1 E:ASP434 2.2 21.1 1.0
OD2 E:ASP434 2.2 21.1 1.0
OD1 E:ASP324 2.4 21.7 1.0
CG E:ASP434 2.5 21.1 1.0
OD2 E:ASP324 2.9 21.7 1.0
NE2 E:HIS86 3.0 19.1 1.0
CG E:ASP324 3.0 21.7 1.0
OE1 E:GLU379 3.5 20.6 1.0
CE E:MET533 3.5 21.0 1.0
CE1 E:HIS86 3.8 19.1 1.0
OE2 E:GLU379 3.9 20.6 1.0
CD E:GLU379 3.9 20.6 1.0
CB E:ASP434 4.0 21.1 1.0
CD2 E:HIS86 4.1 19.1 1.0
NE2 E:HIS534 4.2 21.0 1.0
OE2 E:GLU380 4.5 19.9 1.0
CB E:ASP324 4.5 21.7 1.0
N E:MET435 4.7 20.0 1.0
CB E:ASN325 4.8 20.8 1.0
CA E:ASP434 4.9 21.1 1.0
C E:ASP324 4.9 21.7 1.0
CD2 E:HIS534 5.0 21.0 1.0
OE1 E:GLU380 5.0 19.9 1.0

Reference:

C.M.Ho, X.Li, M.Lai, T.C.Terwilliger, J.R.Beck, J.Wohlschlegel, D.E.Goldberg, A.W.P.Fitzpatrick, Z.H.Zhou. Bottom-Up Structural Proteomics: Cryoem of Protein Complexes Enriched From the Cellular Milieu. Nat.Methods 2019.
ISSN: ESSN 1548-7105
PubMed: 31768063
DOI: 10.1038/S41592-019-0637-Y
Page generated: Tue Oct 29 04:59:46 2024

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