Cobalt in PDB 1epy: T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H

All present enzymatic activity of T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H:
3.2.1.17;

The structure of T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H, PDB code: 1epy was solved by J.W.Wray, W.A.Baase, G.J.Ostheimer, X.-J.Zhang, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	62.385, 62.385, 97.241, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The structure of T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Cobalt atom in the T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H (pdb code 1epy). 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 T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H, PDB code: 1epy:

Cobalt binding site 1 out of 1 in the T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of T4 Lysozyme Mutant, T21H/C54T/C97A/Q141H/T142H within 5.0Å range: probe atom residue distance (Å) B Occ A:Co500 b:19.9 occ:1.00 O A:HOH501 1.9 23.1 1.0 O A:HOH502 2.0 12.4 1.0 NE2 A:HIS21 2.1 15.4 1.0 O A:HOH504 2.2 21.6 1.0 O A:HOH503 2.3 18.9 1.0 NE2 A:HIS142 2.3 8.9 1.0 CE1 A:HIS21 3.0 12.4 1.0 CD2 A:HIS142 3.1 10.7 1.0 CD2 A:HIS21 3.3 14.6 1.0 CE1 A:HIS142 3.3 7.6 1.0 OE2 A:GLU22 3.9 23.9 1.0 CG A:GLU22 4.1 17.4 1.0 NE2 A:GLN105 4.1 11.4 1.0 ND1 A:HIS21 4.1 13.0 1.0 CG A:HIS21 4.3 15.6 1.0 CG A:HIS142 4.3 9.9 1.0 O A:HOH444 4.4 49.0 1.0 ND1 A:HIS142 4.4 13.5 1.0 CD A:GLU22 4.5 28.1 1.0 O A:HOH204 4.6 37.3 1.0 OD2 A:ASP20 4.7 28.7 1.0 O A:HOH467 4.7 52.2 1.0 O A:HOH405 4.8 45.4 1.0

J.W.Wray, W.A.Baase, G.J.Ostheimer, X.J.Zhang, B.W.Matthews. Use of A Non-Rigid Region in T4 Lysozyme to Design An Adaptable Metal-Binding Site. Protein Eng. V. 13 313 2000.
ISSN: ISSN 0269-2139
PubMed: 10835104
DOI: 10.1093/PROTEIN/13.5.313