Cadmium in PDB 1qjw: CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose

All present enzymatic activity of CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose:
3.2.1.91;

The structure of CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose, PDB code: 1qjw was solved by J.-Y.Zou, T.A.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.490, 74.310, 90.710, 90.00, 103.82, 90.00
R / Rfree (%)	17.9 / 20.8

The binding sites of Cadmium atom in the CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose (pdb code 1qjw). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 4 binding sites of Cadmium where determined in the CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose, PDB code: 1qjw:
Jump to Cadmium binding site number: 1; 2; 3; 4;

Cadmium binding site 1 out of 4 in the CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd895 b:20.9 occ:1.00 OE2 A:GLU146 2.4 10.7 1.0 OE1 A:GLU146 2.5 10.6 1.0 O A:HOH2142 2.7 29.7 1.0 CD A:GLU146 2.8 10.3 1.0 OE1 A:GLU208 4.1 23.0 1.0 O A:HOH2060 4.2 24.1 1.0 O A:HOH2061 4.2 13.3 1.0 CG A:GLU146 4.2 10.2 1.0 OE2 A:GLU208 4.4 21.8 1.0 O A:HOH2062 4.4 11.0 1.0 CD A:GLU208 4.7 21.1 1.0

Cadmium binding site 2 out of 4 in the CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd896 b:32.7 occ:1.00 ND1 A:HIS414 2.4 11.9 1.0 OD1 A:ASP412 2.5 9.5 1.0 O A:HOH2318 2.5 15.7 1.0 CE1 A:HIS414 3.2 11.7 1.0 CG A:ASP412 3.2 10.6 1.0 OD2 A:ASP412 3.3 11.8 1.0 CG A:HIS414 3.6 11.0 1.0 OG A:SER413 3.9 16.1 1.0 N A:HIS414 4.0 9.8 1.0 CB A:HIS414 4.0 9.7 1.0 O A:HOH2370 4.2 10.4 1.0 O A:HOH2321 4.4 13.8 1.0 NE2 A:HIS414 4.4 12.3 1.0 N A:SER413 4.5 11.0 1.0 CA A:HIS414 4.5 9.3 1.0 O A:HOH2322 4.5 12.6 1.0 CD2 A:HIS414 4.6 11.8 1.0 CB A:ASP412 4.7 10.3 1.0 CZ2 A:TRP367 4.9 8.2 1.0 C A:SER413 4.9 10.6 1.0 C A:ASP412 4.9 10.8 1.0 NE1 A:TRP367 5.0 8.0 1.0 CB A:SER413 5.0 12.3 1.0

Cadmium binding site 3 out of 4 in the CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd895 b:21.5 occ:1.00 OE2 B:GLU146 2.4 10.2 1.0 OE1 B:GLU146 2.6 10.4 1.0 O B:HOH2131 2.6 21.6 1.0 CD B:GLU146 2.8 10.9 1.0 OE1 B:GLU208 3.8 25.7 1.0 O B:HOH2049 4.1 29.7 1.0 OE2 B:GLU208 4.2 25.6 1.0 CG B:GLU146 4.3 10.5 1.0 CD B:GLU208 4.4 23.6 1.0

Cadmium binding site 4 out of 4 in the CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 4 of CEL6A (Y169F) with A Non-Hydrolysable Cellotetraose within 5.0Å range: probe atom residue distance (Å) B Occ B:Cd896 b:25.7 occ:1.00 ND1 B:HIS414 2.4 11.7 1.0 O B:HOH2297 2.4 15.6 1.0 OD1 B:ASP412 2.5 8.9 1.0 O B:HOH2298 2.7 23.2 1.0 CE1 B:HIS414 3.1 11.4 1.0 CG B:ASP412 3.2 9.5 1.0 OD2 B:ASP412 3.3 10.1 1.0 CG B:HIS414 3.5 11.0 1.0 CB B:HIS414 3.9 9.5 1.0 N B:HIS414 4.0 10.1 1.0 O B:HOH2355 4.1 7.3 1.0 OG B:SER413 4.1 17.0 1.0 O B:HOH2301 4.3 16.2 1.0 NE2 B:HIS414 4.3 12.0 1.0 O B:HOH2300 4.4 27.4 1.0 O B:HOH2302 4.4 12.2 1.0 CA B:HIS414 4.5 9.5 1.0 CD2 B:HIS414 4.5 11.8 1.0 N B:SER413 4.6 10.6 1.0 CB B:ASP412 4.6 9.4 1.0 O B:HOH2085 4.7 24.0 1.0 CZ2 B:TRP367 4.8 7.9 1.0 NE1 B:TRP367 4.9 7.5 1.0 C B:SER413 5.0 10.9 1.0 C B:ASP412 5.0 9.9 1.0

J.-Y.Zou, G.J.Kleywegt, J.Stahlberg, H.Driguez, W.Nerinckx, M.Claeyssens, A.Koivula, T.T.Teeri, T.A.Jones. Crystallographic Evidence For Substrate Ring Distortion and Protein Conformational Changes During Catalysis in Cellobiohydrolase CEL6A From Trichoderma Reesei Structure V. 7 1035 1999.
ISSN: ISSN 0969-2126
PubMed: 10508787
DOI: 10.1016/S0969-2126(99)80171-3