Zinc in PDB 9g2z: Cryo-Em Structure of Irtab in Outward-Occluded State Under Turnover Conditions in Lmng

The structure of Cryo-Em Structure of Irtab in Outward-Occluded State Under Turnover Conditions in Lmng also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the Cryo-Em Structure of Irtab in Outward-Occluded State Under Turnover Conditions in Lmng (pdb code 9g2z). 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 in Outward-Occluded State Under Turnover Conditions in Lmng, PDB code: 9g2z:

Zinc binding site 1 out of 1 in the Cryo-Em Structure of Irtab in Outward-Occluded State Under Turnover Conditions in Lmng


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 in Outward-Occluded State Under Turnover Conditions in Lmng within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1003 b:71.5 occ:1.00 O A:HOH1101 2.0 32.6 1.0 NE2 A:HIS444 2.3 19.6 1.0 NE2 A:HIS439 2.3 17.8 1.0 NE2 A:HIS393 2.3 22.3 1.0 H2 A:HOH1101 2.4 30.4 1.0 H1 A:HOH1101 2.7 30.2 1.0 CE1 A:HIS439 3.1 19.3 1.0 HE1 A:HIS439 3.1 18.4 1.0 CE1 A:HIS444 3.2 17.4 1.0 CD2 A:HIS393 3.2 19.1 1.0 CE1 A:HIS393 3.3 22.7 1.0 CD2 A:HIS444 3.3 15.6 1.0 HE1 A:HIS444 3.3 16.4 1.0 HD2 A:HIS393 3.4 19.7 1.0 HE1 A:HIS393 3.4 20.6 1.0 CD2 A:HIS439 3.4 16.9 1.0 HD2 A:HIS444 3.5 16.5 1.0 HD2 A:HIS439 3.7 17.4 1.0 HG22 A:THR443 4.2 19.2 1.0 ND1 A:HIS439 4.3 19.3 1.0 ND1 A:HIS393 4.3 21.1 1.0 CG A:HIS393 4.4 16.9 1.0 ND1 A:HIS444 4.4 21.7 1.0 HB A:THR443 4.4 18.5 1.0 CG A:HIS444 4.4 11.9 1.0 CG A:HIS439 4.5 18.1 1.0 HG21 A:THR443 4.5 19.1 1.0 CG2 A:THR443 4.7 20.2 1.0

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