Nickel in PDB 6lru: Marsupenaeus Japonicus Ferritin Mutant (T158H)

All present enzymatic activity of Marsupenaeus Japonicus Ferritin Mutant (T158H):
1.16.3.1;

The structure of Marsupenaeus Japonicus Ferritin Mutant (T158H), PDB code: 6lru was solved by G.Zhao, X.Tan, T.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.11 / 2.40
Space group	P 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	117.349, 117.349, 117.349, 90.00, 90.00, 90.00
R / Rfree (%)	13.1 / 18.3

The structure of Marsupenaeus Japonicus Ferritin Mutant (T158H) also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Nickel atom in the Marsupenaeus Japonicus Ferritin Mutant (T158H) (pdb code 6lru). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Marsupenaeus Japonicus Ferritin Mutant (T158H), PDB code: 6lru:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Marsupenaeus Japonicus Ferritin Mutant (T158H)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Marsupenaeus Japonicus Ferritin Mutant (T158H) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni203 b:75.0 occ:0.50 N1 A:IMD205 2.2 48.4 1.0 O A:HOH320 2.3 41.4 1.0 OE1 A:GLU95 2.3 54.8 1.0 H2 A:IMD205 2.5 67.6 1.0 C2 A:IMD205 2.6 56.3 1.0 CD A:GLU95 3.4 14.2 1.0 C5 A:IMD205 3.5 27.1 1.0 OE2 A:GLU95 3.6 23.4 1.0 N3 A:IMD205 3.9 47.5 1.0 H5 A:IMD205 3.9 32.5 1.0 O A:HOH460 4.1 36.7 1.0 C4 A:IMD205 4.3 42.5 1.0 HA3 A:GLY91 4.5 15.0 1.0 HN3 A:IMD205 4.5 57.0 1.0 HA2 A:GLY91 4.8 15.0 1.0 CG A:GLU95 4.8 23.6 1.0 HG2 A:GLU95 4.9 28.3 1.0

Nickel binding site 2 out of 2 in the Marsupenaeus Japonicus Ferritin Mutant (T158H)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Marsupenaeus Japonicus Ferritin Mutant (T158H) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni204 b:36.9 occ:1.00 N1 A:IMD201 2.1 34.6 1.0 OE2 A:GLU58 2.1 24.4 1.0 O A:HOH383 2.3 21.8 1.0 O A:HOH347 2.3 29.9 1.0 O A:HOH303 2.4 31.3 1.0 O A:HOH324 2.5 24.4 1.0 H5 A:IMD201 2.7 21.7 1.0 C5 A:IMD201 2.8 18.1 1.0 CD A:GLU58 3.1 31.0 1.0 C2 A:IMD201 3.3 27.4 1.0 OE1 A:GLU58 3.4 33.6 1.0 HZ1 A:LYS144 3.5 67.9 1.0 HG A:SER141 3.6 35.3 1.0 H2 A:IMD201 3.6 33.0 1.0 OG A:SER141 3.9 29.4 1.0 O A:HOH442 3.9 20.6 1.0 HA A:SER55 3.9 14.2 1.0 O A:HOH450 3.9 32.4 1.0 OE2 A:GLU137 4.1 61.9 1.0 C4 A:IMD201 4.1 25.3 1.0 NZ A:LYS144 4.2 56.5 1.0 HZ2 A:LYS144 4.2 67.9 1.0 OG A:SER55 4.3 12.6 1.0 N3 A:IMD201 4.3 32.0 1.0 O A:HOH330 4.3 19.8 1.0 HZ3 A:LYS144 4.3 67.9 1.0 HB2 A:GLU58 4.4 16.7 1.0 HG A:SER55 4.4 15.2 1.0 CG A:GLU58 4.5 18.9 1.0 HB2 A:SER141 4.6 12.8 1.0 HB3 A:GLU58 4.7 16.7 1.0 O A:HOH314 4.7 42.8 1.0 CB A:GLU58 4.7 13.9 1.0 CA A:SER55 4.8 11.9 1.0 CB A:SER141 4.8 10.6 1.0 O A:HOH332 4.8 23.1 1.0 H4 A:IMD201 4.9 30.4 1.0 HD2 A:LYS144 4.9 49.8 1.0 HG2 A:GLU58 4.9 22.7 1.0 CB A:SER55 5.0 11.6 1.0 HB3 A:SER55 5.0 14.0 1.0 HG3 A:GLU58 5.0 22.7 1.0

X.Tan, H.Chen, C.Gu, J.Zhang, T.Zhang, H.Wang, G.Zhao. Converting Histidine-Induced 3D Protein Arrays in Crystals Into Their 3D Analogues in Solution By Metal Coordination Cross-Linking. Commun Chem 2020.
ISSN: ESSN 2399-3669
DOI: 10.1038/S42004-020-00394-X