Cobalt in PDB 1ugs: Crystal Structure of AY114T Mutant of Co-Type Nitrile Hydratase

All present enzymatic activity of Crystal Structure of AY114T Mutant of Co-Type Nitrile Hydratase:
4.2.1.84;

The structure of Crystal Structure of AY114T Mutant of Co-Type Nitrile Hydratase, PDB code: 1ugs was solved by A.Miyanaga, S.Fushinobu, K.Ito, H.Shoun, T.Wakagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.45 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.517, 65.517, 184.874, 90.00, 90.00, 120.00
R / Rfree (%)	18.1 / 22.5

The binding sites of Cobalt atom in the Crystal Structure of AY114T Mutant of Co-Type Nitrile Hydratase (pdb code 1ugs). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of AY114T Mutant of Co-Type Nitrile Hydratase, PDB code: 1ugs:

Cobalt binding site 1 out of 1 in the Crystal Structure of AY114T Mutant of Co-Type Nitrile Hydratase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of AY114T Mutant of Co-Type Nitrile Hydratase within 5.0Å range: probe atom residue distance (Å) B Occ A:Co301 b:24.3 occ:0.29 N A:SER112 2.1 29.5 1.0 N A:CYS113 2.4 21.6 1.0 SG A:CYS111 2.5 49.1 1.0 SG A:CYS108 2.5 27.8 1.0 CB A:CYS111 2.6 34.5 1.0 SG A:CYS113 2.7 40.7 1.0 C A:CYS111 3.0 33.1 1.0 CA A:SER112 3.1 30.6 1.0 C A:SER112 3.1 25.6 1.0 CA A:CYS111 3.2 30.8 1.0 CB A:CYS113 3.3 29.5 1.0 CA A:CYS113 3.4 22.0 1.0 N A:CYS111 3.6 25.5 1.0 CB A:CYS108 3.7 12.6 1.0 OG A:SER112 4.2 35.4 1.0 O A:CYS111 4.2 37.0 1.0 CB A:SER112 4.2 31.9 1.0 O A:SER112 4.3 24.1 1.0 NH2 B:ARG157 4.4 28.3 1.0 C A:LEU110 4.6 19.4 1.0 O B:HOH381 4.6 28.6 1.0 C A:CYS113 4.7 24.4 1.0 O A:CYS108 4.7 14.7 1.0 CA A:CYS108 4.9 14.7 1.0 O A:CYS113 4.9 25.2 1.0

A.Miyanaga, S.Fushinobu, K.Ito, H.Shoun, T.Wakagi. Mutational and Structural Analysis of Cobalt-Containing Nitrile Hydratase on Substrate and Metal Binding Eur.J.Biochem. V. 271 429 2004.
ISSN: ISSN 0014-2956
PubMed: 14717710
DOI: 10.1046/J.1432-1033.2003.03943.X