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Zinc in PDB 9g2p: Cryo-Em Structure of Irtab 2XEQ Mutant in Outward-Occluded State in Nanodisc

Other elements in 9g2p:

The structure of Cryo-Em Structure of Irtab 2XEQ Mutant in Outward-Occluded State in Nanodisc also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryo-Em Structure of Irtab 2XEQ Mutant in Outward-Occluded State in Nanodisc (pdb code 9g2p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Cryo-Em Structure of Irtab 2XEQ Mutant in Outward-Occluded State in Nanodisc, PDB code: 9g2p:

Zinc binding site 1 out of 1 in 9g2p

Go back to Zinc Binding Sites List in 9g2p
Zinc binding site 1 out of 1 in the Cryo-Em Structure of Irtab 2XEQ Mutant in Outward-Occluded State in Nanodisc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Irtab 2XEQ Mutant in Outward-Occluded State in Nanodisc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1003

b:63.0
occ:1.00
NE2 A:HIS439 2.3 12.7 1.0
NE2 A:HIS393 2.3 12.4 1.0
NE2 A:HIS444 2.3 9.7 1.0
HE1 A:HIS444 3.0 8.8 1.0
CE1 A:HIS444 3.0 8.5 1.0
CE1 A:HIS393 3.1 10.1 1.0
HE1 A:HIS393 3.2 9.8 1.0
CE1 A:HIS439 3.2 12.7 1.0
CD2 A:HIS439 3.3 8.5 1.0
CD2 A:HIS393 3.3 8.2 1.0
HE1 A:HIS439 3.4 11.6 1.0
CD2 A:HIS444 3.5 8.3 1.0
HD2 A:HIS439 3.5 8.9 1.0
HD2 A:HIS393 3.6 8.3 1.0
HD2 A:HIS444 3.8 8.2 1.0
HG22 A:THR443 4.0 9.0 1.0
ND1 A:HIS444 4.3 8.3 1.0
ND1 A:HIS393 4.3 8.7 1.0
HG21 A:THR443 4.3 9.3 1.0
ND1 A:HIS439 4.4 10.8 1.0
CG A:HIS393 4.4 7.0 1.0
CG A:HIS439 4.4 9.0 1.0
CG A:HIS444 4.5 7.6 1.0
HB A:THR443 4.5 8.5 1.0
CG2 A:THR443 4.6 9.3 1.0
HD1 A:HIS444 5.0 8.3 1.0

Reference:

I.Gonda, S.Sorrentino, L.Galazzo, N.P.Lichti, F.M.Arnold, A.R.Mehdipour, E.Bordignon, M.A.Seeger. The Mycobacterial Abc Transporter Irtab Employs A Membrane-Facing Crevice For Siderophore-Mediated Iron Uptake Nature 2024.
ISSN: ESSN 1476-4687
DOI: 10.1038/S41467-024-55136-7
Page generated: Sun Feb 9 01:21:38 2025

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