Nickel in PDB 8gf5: Mcrd Binds Asymmetrically to Methyl-Coenzyme M Reductase Improving Active Site Accessibility During Assembly

All present enzymatic activity of Mcrd Binds Asymmetrically to Methyl-Coenzyme M Reductase Improving Active Site Accessibility During Assembly:
2.8.4.1;

The binding sites of Nickel atom in the Mcrd Binds Asymmetrically to Methyl-Coenzyme M Reductase Improving Active Site Accessibility During Assembly (pdb code 8gf5). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Mcrd Binds Asymmetrically to Methyl-Coenzyme M Reductase Improving Active Site Accessibility During Assembly, PDB code: 8gf5:

Nickel binding site 1 out of 1 in the Mcrd Binds Asymmetrically to Methyl-Coenzyme M Reductase Improving Active Site Accessibility During Assembly


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Mcrd Binds Asymmetrically to Methyl-Coenzyme M Reductase Improving Active Site Accessibility During Assembly within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni602 b:59.0 occ:1.00 NI A:F43602 0.0 59.0 1.0 ND A:F43602 2.0 59.0 1.0 NC A:F43602 2.1 59.0 1.0 NB A:F43602 2.1 59.0 1.0 NA A:F43602 2.1 59.0 1.0 C4B A:F43602 2.9 59.0 1.0 C1A A:F43602 3.0 59.0 1.0 C1C A:F43602 3.0 59.0 1.0 NE2 B:GLN161 3.0 60.0 1.0 C4D A:F43602 3.0 59.0 1.0 C1D A:F43602 3.1 59.0 1.0 C4C A:F43602 3.1 59.0 1.0 HHA1 A:F43602 3.1 59.0 1.0 C1B A:F43602 3.2 59.0 1.0 C1 A:COM601 3.2 57.1 1.0 HHB1 A:F43602 3.2 59.0 1.0 S1 A:COM601 3.2 57.1 1.0 CHA A:F43602 3.2 59.0 1.0 C4A A:F43602 3.3 59.0 1.0 CHC A:F43602 3.3 59.0 1.0 H4D A:F43602 3.3 59.0 1.0 CHB A:F43602 3.4 59.0 1.0 CHD A:F43602 3.5 59.0 1.0 H4A A:F43602 3.7 59.0 1.0 H5B A:F43602 3.7 59.0 1.0 N5B A:F43602 3.8 59.0 1.0 CD B:GLN161 3.9 60.0 1.0 OE1 B:GLN161 4.0 60.0 1.0 HAB1 A:F43602 4.2 59.0 1.0 HHC A:F43602 4.2 59.0 1.0 HHA2 A:F43602 4.2 59.0 1.0 C2 A:COM601 4.2 57.1 1.0 C3B A:F43602 4.3 59.0 1.0 C2D A:F43602 4.3 59.0 1.0 C3D A:F43602 4.3 59.0 1.0 C2A A:F43602 4.3 59.0 1.0 HAA2 A:F43602 4.3 59.0 1.0 HHB2 A:F43602 4.3 59.0 1.0 C2C A:F43602 4.3 59.0 1.0 OH A:TYR346 4.4 56.1 1.0 C3A A:F43602 4.4 59.0 1.0 C3C A:F43602 4.4 59.0 1.0 C2B A:F43602 4.4 59.0 1.0 OH C:TYR365 4.5 52.7 1.0 H2D A:F43602 4.6 59.0 1.0 H3D A:F43602 4.6 59.0 1.0 H5C2 A:F43602 4.7 59.0 1.0 CAA A:F43602 4.7 59.0 1.0 CAB A:F43602 4.7 59.0 1.0 HAA1 A:F43602 4.8 59.0 1.0 H8C2 A:F43602 4.9 59.0 1.0 H9A2 A:F43602 4.9 59.0 1.0 C6B A:F43602 4.9 59.0 1.0 C7D A:F43602 4.9 59.0 1.0 HBB2 A:F43602 4.9 59.0 1.0 O2S A:COM601 4.9 57.1 1.0 H2C A:F43602 5.0 59.0 1.0

G.L.Chadwick, A.M.N.Joiner, S.Ramesh, D.A.Mitchell, D.D.Nayak. Mcrd Binds Asymmetrically to Methyl-Coenzyme M Reductase Improving Active-Site Accessibility During Assembly. Proc.Natl.Acad.Sci.Usa V. 120 15120 2023.
ISSN: ESSN 1091-6490
PubMed: 37307484
DOI: 10.1073/PNAS.2302815120