Cobalt in PDB 4q3x: Crystal Structure of C. Violaceum Phenylalanine Hydroxylase D139N Mutation

All present enzymatic activity of Crystal Structure of C. Violaceum Phenylalanine Hydroxylase D139N Mutation:
1.14.16.1;

The structure of Crystal Structure of C. Violaceum Phenylalanine Hydroxylase D139N Mutation, PDB code: 4q3x was solved by J.A.Ronau, M.M.Abu-Omar, C.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.70 / 1.35
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	36.804, 38.534, 47.818, 76.53, 73.09, 85.55
R / Rfree (%)	16.1 / 20

The binding sites of Cobalt atom in the Crystal Structure of C. Violaceum Phenylalanine Hydroxylase D139N Mutation (pdb code 4q3x). 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 C. Violaceum Phenylalanine Hydroxylase D139N Mutation, PDB code: 4q3x:

Cobalt binding site 1 out of 1 in the Crystal Structure of C. Violaceum Phenylalanine Hydroxylase D139N Mutation


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 C. Violaceum Phenylalanine Hydroxylase D139N Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Co301 b:7.2 occ:1.00 NE2 A:HIS138 2.0 7.0 1.0 O A:HOH404 2.1 12.4 1.0 NE2 A:HIS143 2.1 6.6 1.0 O A:HOH403 2.1 10.7 1.0 OE2 A:GLU184 2.1 8.4 1.0 OE1 A:GLU184 2.2 7.2 1.0 CD A:GLU184 2.5 6.9 1.0 CE1 A:HIS138 3.0 6.9 1.0 CD2 A:HIS143 3.1 8.0 1.0 CE1 A:HIS143 3.1 6.6 1.0 CD2 A:HIS138 3.1 6.8 1.0 O A:HOH402 3.9 12.8 1.0 CG A:GLU184 4.0 7.0 1.0 ND1 A:HIS138 4.1 7.2 1.0 ND1 A:HIS143 4.2 7.8 1.0 CG A:HIS138 4.2 6.0 1.0 CG A:HIS143 4.2 7.3 1.0 O A:HOH476 4.2 25.3 1.0 OD1 A:ASN139 4.3 14.1 1.0 O A:HOH487 4.4 25.8 1.0 CB A:ALA199 4.6 7.8 1.0 CB A:GLU184 4.9 6.6 1.0

J.A.Ronau, L.N.Paul, J.E.Fuchs, K.R.Liedl, M.M.Abu-Omar, C.Das. A Conserved Acidic Residue in Phenylalanine Hydroxylase Contributes to Cofactor Affinity and Catalysis. Biochemistry V. 53 6834 2014.
ISSN: ISSN 0006-2960
PubMed: 25295853
DOI: 10.1021/BI500734H