Copper in PDB 3zud: 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: 3zud 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)	27.81 / 1.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.500, 87.300, 37.300, 90.00, 104.70, 90.00
R / Rfree (%)	15.5 / 17.9

The binding sites of Copper atom in the Thermoascus GH61 Isozyme A (pdb code 3zud). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Thermoascus GH61 Isozyme A, PDB code: 3zud:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 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:16.5 occ:0.60 CU A:CU301 0.0 16.5 0.6 CU A:CU301 1.6 15.4 0.1 ND1 A:HIC1 1.9 20.1 1.0 NE2 A:HIS86 2.0 17.5 1.0 O1 A:PEG306 2.1 29.8 0.3 N A:HIC1 2.2 19.6 1.0 CD2 A:HIS86 2.8 17.1 1.0 O A:HOH574 2.9 33.2 1.0 CG A:HIC1 2.9 20.8 1.0 CE1 A:HIC1 2.9 21.5 1.0 OH A:TYR175 2.9 13.9 1.0 CE1 A:HIS86 3.1 16.2 1.0 C1 A:PEG306 3.2 30.7 0.3 CA A:HIC1 3.2 18.9 1.0 CB A:HIC1 3.4 19.7 1.0 OE1 A:GLN173 3.9 16.2 1.0 CG A:HIS86 4.0 15.1 1.0 NE2 A:HIC1 4.0 22.1 1.0 CD2 A:HIC1 4.1 21.4 1.0 CZ A:TYR175 4.1 12.2 1.0 ND1 A:HIS86 4.1 15.3 1.0 C2 A:PEG306 4.6 32.4 0.3 C A:HIC1 4.6 18.1 1.0 CE2 A:TYR175 4.6 12.7 1.0 CG A:PRO83 4.9 16.4 1.0 NE2 A:HIS164 5.0 15.9 1.0 O A:HIC1 5.0 19.4 1.0

Copper binding site 2 out of 4 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 A:Cu301 b:15.4 occ:0.15 CU A:CU301 0.0 15.4 0.1 O1 A:PEG306 1.6 29.8 0.3 CU A:CU301 1.6 16.5 0.6 NE2 A:HIS86 2.1 17.5 1.0 C1 A:PEG306 2.2 30.7 0.3 O A:HOH574 2.4 33.2 1.0 CE1 A:HIS86 2.5 16.2 1.0 ND1 A:HIC1 2.6 20.1 1.0 CE1 A:HIC1 3.2 21.5 1.0 CD2 A:HIS86 3.4 17.1 1.0 C2 A:PEG306 3.5 32.4 0.3 N A:HIC1 3.6 19.6 1.0 CG A:HIC1 3.8 20.8 1.0 ND1 A:HIS86 3.8 15.3 1.0 OH A:TYR175 4.2 13.9 1.0 OE1 A:GLN173 4.2 16.2 1.0 CG A:HIS86 4.2 15.1 1.0 O2 A:PEG306 4.3 34.1 0.3 CE1 A:HIS164 4.4 13.9 1.0 CB A:HIC1 4.4 19.7 1.0 NE2 A:HIC1 4.5 22.1 1.0 NE2 A:HIS164 4.6 15.9 1.0 CA A:HIC1 4.6 18.9 1.0 CD2 A:HIC1 4.7 21.4 1.0

Copper binding site 3 out of 4 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 3 of Thermoascus GH61 Isozyme A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu302 b:19.6 occ:0.60 NE2 A:HIS87 1.9 14.0 0.5 NE2 A:HIS87 2.0 14.3 0.5 O5 A:TAM305 2.1 34.9 1.0 O6 A:TAM305 2.2 28.6 1.0 CE1 A:HIS87 2.3 14.9 0.5 N A:TAM305 2.3 35.5 1.0 CE1 A:HIS87 2.9 15.3 0.5 O A:HOH402 2.9 40.6 1.0 C5 A:TAM305 2.9 35.2 1.0 C6 A:TAM305 2.9 32.4 1.0 CD2 A:HIS87 3.0 13.1 0.5 C A:TAM305 3.1 35.5 1.0 CD2 A:HIS87 3.3 13.9 0.5 C3 A:TAM305 3.3 34.8 1.0 C2 A:TAM305 3.3 35.4 1.0 ND1 A:HIS87 3.6 14.0 0.5 O A:GLY127 3.8 15.7 1.0 ND1 A:HIS87 4.0 14.2 0.5 CG A:HIS87 4.0 13.2 0.5 CG A:HIS87 4.1 12.8 0.5 O A:HOH443 4.2 35.7 1.0 CG A:PRO126 4.2 16.9 1.0 O A:ASP84 4.3 16.6 1.0 O A:HOH472 4.4 25.5 1.0 C1 A:TAM305 4.5 36.4 1.0 OD1 A:ASP132 4.6 17.6 1.0 CD A:PRO126 4.7 16.7 1.0 C A:GLY127 5.0 14.3 1.0

Copper binding site 4 out of 4 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 4 of Thermoascus GH61 Isozyme A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:24.2 occ:0.20 OD1 A:ASP189 2.0 25.1 1.0 O A:HOH564 2.0 51.6 1.0 O A:HOH563 2.4 49.1 1.0 CG A:ASP189 2.7 23.0 1.0 OD2 A:ASP189 2.8 24.9 1.0 CB A:ASP189 4.2 21.4 1.0 O A:HOH524 4.2 34.0 1.0 C A:GLY228 4.5 32.0 1.0 O A:GLY228 4.6 32.9 1.0 CA A:ASP189 4.8 21.0 1.0 N A:ASP189 4.9 20.6 1.0 O A:THR148 5.0 20.7 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