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Zinc in PDB 1hyi: Solution Structure of the EEA1 Fyve Domain Complexed with Inositol 1,3-Bisphosphate

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the EEA1 Fyve Domain Complexed with Inositol 1,3-Bisphosphate (pdb code 1hyi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of the EEA1 Fyve Domain Complexed with Inositol 1,3-Bisphosphate, PDB code: 1hyi:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1hyi

Go back to Zinc Binding Sites List in 1hyi
Zinc binding site 1 out of 2 in the Solution Structure of the EEA1 Fyve Domain Complexed with Inositol 1,3-Bisphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the EEA1 Fyve Domain Complexed with Inositol 1,3-Bisphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn66

b:0.0
occ:1.00
H A:CYS36 2.1 0.0 1.0
SG A:CYS36 2.4 0.0 1.0
SG A:CYS12 2.4 0.0 1.0
SG A:CYS39 2.4 0.0 1.0
HB2 A:CYS39 2.5 0.0 1.0
HG A:CYS15 2.5 0.0 1.0
SG A:CYS15 2.5 0.0 1.0
HB3 A:CYS15 2.9 0.0 1.0
HB3 A:CYS36 2.9 0.0 1.0
H A:CYS15 2.9 0.0 1.0
CB A:CYS39 2.9 0.0 1.0
HG A:CYS12 3.0 0.0 1.0
N A:CYS36 3.0 0.0 1.0
CB A:CYS36 3.1 0.0 1.0
HG A:CYS39 3.2 0.0 1.0
H A:CYS39 3.2 0.0 1.0
CB A:CYS15 3.2 0.0 1.0
HG A:CYS36 3.3 0.0 1.0
HB1 A:ALA14 3.3 0.0 1.0
HB2 A:CYS12 3.3 0.0 1.0
CB A:CYS12 3.4 0.0 1.0
HB3 A:CYS12 3.6 0.0 1.0
HB3 A:CYS39 3.6 0.0 1.0
N A:CYS15 3.6 0.0 1.0
CA A:CYS36 3.6 0.0 1.0
HA A:PHE35 3.7 0.0 1.0
N A:CYS39 3.8 0.0 1.0
H A:GLY16 4.0 0.0 1.0
HD1 A:PHE35 4.0 0.0 1.0
CA A:CYS39 4.0 0.0 1.0
C A:PHE35 4.1 0.0 1.0
HB2 A:CYS36 4.1 0.0 1.0
CA A:CYS15 4.1 0.0 1.0
HB2 A:CYS15 4.1 0.0 1.0
HB3 A:PHE35 4.1 0.0 1.0
HB3 A:GLU38 4.1 0.0 1.0
HG2 A:LYS17 4.2 0.0 1.0
O A:CYS36 4.3 0.0 1.0
CA A:PHE35 4.3 0.0 1.0
C A:CYS36 4.3 0.0 1.0
CB A:ALA14 4.3 0.0 1.0
H A:ALA14 4.3 0.0 1.0
HA A:CYS39 4.5 0.0 1.0
H A:GLU38 4.5 0.0 1.0
HA A:CYS36 4.6 0.0 1.0
C A:ALA14 4.6 0.0 1.0
H A:LYS17 4.6 0.0 1.0
HB3 A:ALA14 4.6 0.0 1.0
N A:GLY16 4.7 0.0 1.0
CB A:PHE35 4.7 0.0 1.0
CA A:CYS12 4.8 0.0 1.0
H A:MET13 4.8 0.0 1.0
OE1 A:GLU38 4.8 0.0 1.0
N A:ALA14 4.8 0.0 1.0
C A:CYS15 4.8 0.0 1.0
H A:SER40 4.9 0.0 1.0
CA A:ALA14 4.9 0.0 1.0
HG3 A:LYS17 4.9 0.0 1.0
C A:GLU38 4.9 0.0 1.0
CD1 A:PHE35 5.0 0.0 1.0
HA A:CYS15 5.0 0.0 1.0

Zinc binding site 2 out of 2 in 1hyi

Go back to Zinc Binding Sites List in 1hyi
Zinc binding site 2 out of 2 in the Solution Structure of the EEA1 Fyve Domain Complexed with Inositol 1,3-Bisphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the EEA1 Fyve Domain Complexed with Inositol 1,3-Bisphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn67

b:0.0
occ:1.00
HG A:CYS59 2.0 0.0 1.0
HB3 A:CYS59 2.4 0.0 1.0
SG A:CYS59 2.7 0.0 1.0
SG A:CYS28 2.8 0.0 1.0
SG A:CYS31 2.9 0.0 1.0
SG A:CYS56 2.9 0.0 1.0
CB A:CYS59 3.0 0.0 1.0
H A:CYS56 3.0 0.0 1.0
HE2 A:PHE35 3.2 0.0 1.0
HB3 A:CYS56 3.3 0.0 1.0
HB2 A:CYS31 3.4 0.0 1.0
H A:CYS59 3.5 0.0 1.0
HB2 A:CYS59 3.5 0.0 1.0
HB2 A:CYS28 3.5 0.0 1.0
H A:CYS31 3.6 0.0 1.0
HG A:CYS31 3.6 0.0 1.0
CB A:CYS28 3.6 0.0 1.0
CB A:CYS56 3.7 0.0 1.0
HG A:CYS28 3.7 0.0 1.0
HB3 A:CYS28 3.8 0.0 1.0
HG A:CYS56 3.8 0.0 1.0
CB A:CYS31 3.8 0.0 1.0
N A:CYS56 3.9 0.0 1.0
HD21 A:ASN33 3.9 0.0 1.0
HB A:VAL55 4.0 0.0 1.0
CE2 A:PHE35 4.1 0.0 1.0
N A:CYS59 4.2 0.0 1.0
CA A:CYS59 4.2 0.0 1.0
HB2 A:GLN30 4.3 0.0 1.0
CA A:CYS56 4.4 0.0 1.0
HZ A:PHE35 4.4 0.0 1.0
HB3 A:CYS31 4.4 0.0 1.0
N A:CYS31 4.5 0.0 1.0
HB3 A:ALA58 4.5 0.0 1.0
HB2 A:CYS56 4.6 0.0 1.0
CZ A:PHE35 4.7 0.0 1.0
HB3 A:GLN30 4.7 0.0 1.0
HA A:CYS59 4.8 0.0 1.0
HB2 A:ASN33 4.8 0.0 1.0
HA A:VAL55 4.8 0.0 1.0
CA A:CYS31 4.8 0.0 1.0
ND2 A:ASN33 4.9 0.0 1.0
C A:VAL55 4.9 0.0 1.0
C A:CYS56 4.9 0.0 1.0
O A:CYS56 5.0 0.0 1.0
H A:PHE60 5.0 0.0 1.0
CB A:VAL55 5.0 0.0 1.0

Reference:

T.Kutateladze, M.Overduin. Structural Mechanism of Endosome Docking By the Fyve Domain. Science V. 291 1793 2001.
ISSN: ISSN 0036-8075
PubMed: 11230696
DOI: 10.1126/SCIENCE.291.5509.1793
Page generated: Sun Oct 13 02:42:16 2024

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