Hypocrea jecorina Cel7A in complex with (S)-dihydroxy-phenanthrenolol

A Study of the Chiral Recognition Mechanisms of Cellobiohydrolase Cel7A for Ligands Based on the Beta-Blocker Motif: Crystal Structures, Microcalorimetry and Computational Modelling of Cel7A-Inhibitor Complexes.

CELLOBIOHYDROLASE CEL7A, EXOGLUCANASE I, EXOCELLOBIOHYDROLASE I, CBHI, 1,4-BETA-CELLOBIOHYDROLASE

SYNONYM FOR STRAIN IS TRICHODERMA REESEI, WHICH IS A CLONAL DERIVATIVE OF H. JECORINA

POLYETHYLENE GLYCOL MONOMETHYL ETHER, GLYCEROL, COBALT CHLORIDE, SODIUM ACETATE PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298 K

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 23 STRUCTURES

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 18 STRUCTURES

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES

C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I (CT -CBH I) (NMR, MINIMIZED MEAN STRUCTURE)

1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I ( CELLULASE)

CELLOBIOHYDROLASE CEL7A (E223S, A224H, L225V, T226A, D262G)MUTANT

CELLOBIOHYDROLASE CEL7A WITH DISULPHIDE BRIDGE ADDED ACROSSEXO-LOOP BY MUTATIONS D241C AND D249C

CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245 -252 ANDBOUND NON-HYDROLYSABLE CELLOTETRAOSE

C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I (CT -CBH I) (NMR,41 SIMULATED ANNEALING STRUCTURES)

ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE

HYPOCREA JECORINA CEL7A E212Q MUTANT IN COMPLEX WITH P-NITROPHENYL CELLOBIOSIDE

HYPOCREA JECORINA CEL7A IN COMPLEX WITH (R )-DIHYDROXY-PHENANTHRENOLOL

ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOUND IN THE ACTIVE SITE

ACTIVE-SITE MUTANT D214N DETERMINED AT PH 6.0 WITH NO LIGAND BOUND IN THE ACTIVE SITE

CBH1 (E217Q) IN COMPLEX WITH CELLOHEXAOSE AND CELLOBIOSE

THEORETICAL MODEL OF CBH1 IN COMPLEX WITH A CELLULOSE NANOMER

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

BIOLOGICAL CONVERSION OF CELLULOSE TO GLUCOSE
PCA A 1 UNI P62694 GLN 18 MODIFIED RESIDUE

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ALTERNATE CONFORMATIONS WERE MODELLED FOR RESIDUES A 7, 13, 47, 55, 98, 111, 114, 119, 159, 194, 195, 15, 246, 247, 249, 253, 254, 328, 342, 357, 371, 388, 407.

HYDROLASE, GLYCOSIDASE, GLYCOPROTEIN, CARBOHYDRATE METABOLISM, POLYSACCHARIDE DEGRADATION, PYRROLIDONE CARBOXYLIC ACID, HYDROLASE(O-GLYCOSYL), CELLULOSE DEAGRADATION, CHIRAL SEPARATION, CELLULOSE DEGRADATION