Copper in PDB 2yet: Thermoascus GH61 Isozyme A

All present enzymatic activity of Thermoascus GH61 Isozyme A:
3.2.1.4;

The structure of Thermoascus GH61 Isozyme A, PDB code: 2yet was solved by H.Otten, R.J.Quinlan, M.D.Sweeney, J.-C.N.Poulsen, K.S.Johansen, K.B.R.M.Krogh, C.I.Joergensen, M.Tovborg, A.Anthonsen, T.Tryfona, C.P.Walter, P.Dupree, F.Xu, G.J.Davies, P.H.Walton, L.Lo Leggio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.33 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.404, 88.467, 70.324, 90.00, 103.41, 90.00
R / Rfree (%)	14.4 / 18.5

The binding sites of Copper atom in the Thermoascus GH61 Isozyme A (pdb code 2yet). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Thermoascus GH61 Isozyme A, PDB code: 2yet:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Thermoascus GH61 Isozyme A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Thermoascus GH61 Isozyme A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:24.7 occ:0.20 ND1 A:HIC1 2.1 29.3 1.0 O A:HOH2263 2.2 33.6 1.0 NE2 A:HIS86 2.3 17.7 1.0 N A:HIC1 2.4 24.3 1.0 O A:HOH2001 2.7 30.0 0.5 OH A:TYR175 2.8 14.2 1.0 CD2 A:HIS86 2.8 15.8 1.0 CG A:HIC1 3.0 28.5 1.0 CE1 A:HIC1 3.1 31.0 1.0 CA A:HIC1 3.3 20.7 1.0 CB A:HIC1 3.4 24.8 1.0 CE1 A:HIS86 3.5 16.2 1.0 OE1 A:GLN173 3.8 13.9 1.0 CZ A:TYR175 4.0 11.6 1.0 CG A:HIS86 4.1 14.2 1.0 CD2 A:HIC1 4.2 31.1 1.0 NE2 A:HIC1 4.2 31.9 1.0 ND1 A:HIS86 4.4 14.9 1.0 CE2 A:TYR175 4.6 10.1 1.0 O A:HOH2250 4.7 29.8 1.0 C A:HIC1 4.7 17.6 1.0 CE1 A:TYR175 4.9 10.0 1.0 CG A:PRO83 4.9 13.6 1.0 CD A:GLN173 4.9 13.3 1.0 CE1 A:HIS164 5.0 12.5 1.0

Copper binding site 2 out of 2 in the Thermoascus GH61 Isozyme A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Thermoascus GH61 Isozyme A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:24.7 occ:0.20 ND1 B:HIC1 2.0 26.6 1.0 O B:HOH2239 2.2 35.5 1.0 NE2 B:HIS86 2.3 15.9 1.0 N B:HIC1 2.4 17.5 1.0 O B:HOH2290 2.5 46.1 1.0 OH B:TYR175 2.8 12.7 1.0 CD2 B:HIS86 2.9 13.0 1.0 CG B:HIC1 3.0 23.9 1.0 CE1 B:HIC1 3.0 28.0 1.0 CA B:HIC1 3.3 16.3 1.0 CB B:HIC1 3.4 20.1 1.0 CE1 B:HIS86 3.5 12.1 1.0 OE1 B:GLN173 3.9 13.3 1.0 CZ B:TYR175 3.9 11.3 1.0 NE2 B:HIC1 4.1 28.9 1.0 CD2 B:HIC1 4.1 26.8 1.0 CG B:HIS86 4.2 12.4 1.0 ND1 B:HIS86 4.4 13.2 1.0 O B:HOH2271 4.4 47.5 1.0 CE2 B:TYR175 4.5 10.9 1.0 O B:HOH2228 4.5 34.8 1.0 C B:HIC1 4.7 13.1 1.0 CE1 B:TYR175 4.9 11.1 1.0 CE1 B:HIS164 5.0 12.0 1.0 CG B:PRO83 5.0 12.8 1.0

R.J.Quinlan, M.D.Sweeney, L.Lo Leggio, H.Otten, J.-C.N.Poulsen, K.S.Johansen, K.B.R.M.Krogh, C.I.Jorgensen, M.Tovborg, A.Anthonsen, T.Tryfona, C.P.Walter, P.Dupree, F.Xu, G.J.Davies, P.H.Walton. Insights Into the Oxidative Degradation of Cellulose By A Copper Metalloenzyme That Exploits Biomass Components. Proc.Natl.Acad.Sci.Usa V. 108 15079 2011.
ISSN: ISSN 0027-8424
PubMed: 21876164
DOI: 10.1073/PNAS.1105776108