Zinc in PDB 1b2x: Barnase Wildtype Structure at pH 7.5 From A CRYO_COOLED Crystal at 100K

All present enzymatic activity of Barnase Wildtype Structure at pH 7.5 From A CRYO_COOLED Crystal at 100K:
3.1.27.3;

The structure of Barnase Wildtype Structure at pH 7.5 From A CRYO_COOLED Crystal at 100K, PDB code: 1b2x was solved by P.Harrison, C.K.Vaughan, A.M.Buckle, A.R.Fersht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.80 / 1.80
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	57.630, 57.630, 80.980, 90.00, 90.00, 120.00
R / Rfree (%)	17.3 / 23.6

The binding sites of Zinc atom in the Barnase Wildtype Structure at pH 7.5 From A CRYO_COOLED Crystal at 100K (pdb code 1b2x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Barnase Wildtype Structure at pH 7.5 From A CRYO_COOLED Crystal at 100K, PDB code: 1b2x:

Zinc binding site 1 out of 1 in the Barnase Wildtype Structure at pH 7.5 From A CRYO_COOLED Crystal at 100K


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Barnase Wildtype Structure at pH 7.5 From A CRYO_COOLED Crystal at 100K within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn384 b:11.8 occ:1.00 O A:HOH133 2.1 7.7 1.0 ND1 C:HIS18 2.1 11.5 1.0 CE1 C:HIS18 2.9 10.6 1.0 CG C:HIS18 3.2 10.3 1.0 CB C:HIS18 3.7 8.7 1.0 O A:LEU33 3.8 8.1 1.0 O C:TYR17 4.1 8.2 1.0 NE2 C:HIS18 4.1 9.1 1.0 O A:VAL45 4.2 13.8 1.0 O C:HOH461 4.2 18.1 1.0 CD2 C:HIS18 4.3 10.4 1.0 C C:TYR17 4.5 9.7 1.0 CA A:VAL45 4.6 10.0 1.0 CB A:VAL45 4.7 9.7 1.0 O C:HOH428 4.7 12.7 1.0 N C:HIS18 4.8 7.5 1.0 C A:VAL45 4.9 12.0 1.0 CA C:HIS18 4.9 8.1 1.0 O C:THR16 4.9 13.5 1.0 C A:LEU33 5.0 8.5 1.0

C.K.Vaughan, P.Harryson, A.M.Buckle, A.R.Fersht. A Structural Double-Mutant Cycle: Estimating the Strength of A Buried Salt Bridge in Barnase. Acta Crystallogr.,Sect.D V. 58 591 2002.
ISSN: ISSN 0907-4449
PubMed: 11914482
DOI: 10.1107/S0907444902001567