Zinc in PDB 3rzv: The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh

The structure of The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh, PDB code: 3rzv was solved by C.W.Davies, C.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.47 / 1.67
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	53.437, 53.437, 128.828, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 20.5

The binding sites of Zinc atom in the The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh (pdb code 3rzv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh, PDB code: 3rzv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:22.9 occ:1.00 OD2 A:ASP348 1.9 21.0 1.0 OD1 A:ASP309 1.9 23.8 1.0 NE2 A:HIS337 2.1 23.0 1.0 NE2 A:HIS335 2.1 18.2 1.0 CG A:ASP348 2.7 21.1 1.0 OD1 A:ASP348 2.8 20.2 1.0 CG A:ASP309 2.8 30.3 1.0 CD2 A:HIS337 3.0 23.6 1.0 OD2 A:ASP309 3.1 28.4 1.0 CE1 A:HIS335 3.1 20.0 1.0 CD2 A:HIS335 3.1 24.0 1.0 CE1 A:HIS337 3.2 22.9 1.0 O A:HOH30 3.8 32.1 1.0 OG A:SER345 3.9 20.8 1.0 CB A:ASP348 4.1 17.1 1.0 CG A:HIS337 4.2 23.8 1.0 CB A:ASP309 4.2 28.6 1.0 ND1 A:HIS335 4.2 21.1 1.0 ND1 A:HIS337 4.2 24.6 1.0 CG A:HIS335 4.3 22.8 1.0 O A:PHE343 4.4 21.5 1.0 CB A:SER345 4.6 21.2 1.0 CA A:ASP309 4.6 28.0 1.0 N A:SER345 4.6 19.5 1.0 O A:ASP309 4.6 32.7 1.0 C A:ASP309 4.8 34.2 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of A E280A Mutant of the Catalytic Domain of Amsh within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:24.0 occ:1.00 NE2 A:HIS396 2.0 20.6 1.0 NE2 A:HIS398 2.0 23.9 1.0 NE2 A:HIS350 2.1 26.6 1.0 SG A:CYS390 2.3 24.5 1.0 CE1 A:HIS396 2.9 20.5 1.0 CE1 A:HIS350 3.0 27.0 1.0 CE1 A:HIS398 3.0 26.9 1.0 CD2 A:HIS398 3.1 24.1 1.0 CD2 A:HIS396 3.1 20.3 1.0 CD2 A:HIS350 3.1 23.9 1.0 CB A:CYS390 3.3 24.0 1.0 ND1 A:HIS396 4.0 23.1 1.0 O A:HOH71 4.1 37.5 1.0 ND1 A:HIS398 4.1 24.0 1.0 ND1 A:HIS350 4.1 23.9 1.0 CG A:HIS396 4.2 20.9 1.0 OE1 A:GLN392 4.2 33.9 1.0 CG A:HIS398 4.2 23.4 1.0 CG A:HIS350 4.2 21.3 1.0 OG A:SER346 4.4 24.8 1.0 CD1 A:ILE387 4.4 21.9 1.0 CB A:GLN392 4.5 26.2 1.0 CD A:GLN392 4.7 28.5 1.0 CA A:CYS390 4.7 25.8 1.0 CG A:GLN392 4.9 31.3 1.0 O A:HOH117 4.9 35.7 1.0

C.W.Davies, L.N.Paul, M.I.Kim, C.Das. Structural and Thermodynamic Comparison of the Catalytic Domain of Amsh and Amsh-Lp: Nearly Identical Fold But Different Stability. J.Mol.Biol. V. 413 416 2011.
ISSN: ISSN 0022-2836
PubMed: 21888914
DOI: 10.1016/J.JMB.2011.08.029