6YN7
Crystal Structure of AHE enzyme from Alicyclobacillus herbarius
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0030245 | biological_process | cellulose catabolic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008422 | molecular_function | beta-glucosidase activity |
B | 0030245 | biological_process | cellulose catabolic process |
C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008422 | molecular_function | beta-glucosidase activity |
C | 0030245 | biological_process | cellulose catabolic process |
D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008422 | molecular_function | beta-glucosidase activity |
D | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | PHE8 |
A | GLN10 |
A | HIS446 |
A | GLN449 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | HIS110 |
A | ASP157 |
A | GLY158 |
A | ASP160 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ARG62 |
A | TYR63 |
A | ARG64 |
A | GLU65 |
C | ARG64 |
A | HIS61 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | HIS185 |
A | ASP187 |
A | GLU190 |
A | HOH624 |
B | GLN127 |
B | HIS185 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | ILE290 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | GLU253 |
A | ARG258 |
A | HOH607 |
C | ARG258 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | PHE117 |
A | ASP160 |
A | GLN217 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue NI A 509 |
Chain | Residue |
A | GLU29 |
A | HIS61 |
C | GLU29 |
C | HIS61 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue PGE A 510 |
Chain | Residue |
A | VAL180 |
A | HOH643 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue EDO B 501 |
Chain | Residue |
A | ASP276 |
B | GLN127 |
B | ASP131 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | VAL27 |
B | HIS28 |
B | ARG32 |
B | ASP38 |
B | HOH637 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | HIS110 |
B | GLY158 |
B | ASP160 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue NI B 504 |
Chain | Residue |
B | GLU29 |
B | HIS61 |
D | GLU29 |
D | HIS61 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue PGE B 505 |
Chain | Residue |
B | TRP342 |
B | SER345 |
D | EDO501 |
site_id | AD6 |
Number of Residues | 9 |
Details | binding site for residue PEG B 506 |
Chain | Residue |
B | ARG249 |
B | GLU253 |
B | ARG258 |
B | GLY259 |
B | TYR260 |
B | PRO261 |
B | GLN262 |
D | ARG258 |
D | HOH633 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue EDO C 501 |
Chain | Residue |
C | EDO502 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue EDO C 502 |
Chain | Residue |
C | VAL27 |
C | HIS28 |
C | ARG32 |
C | GLY33 |
C | GLU34 |
C | EDO501 |
site_id | AD9 |
Number of Residues | 1 |
Details | binding site for residue EDO C 503 |
Chain | Residue |
C | GLU72 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue EDO C 504 |
Chain | Residue |
C | GLU167 |
C | GLU356 |
C | GLU409 |
C | HOH607 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue EDO C 505 |
Chain | Residue |
C | GLU34 |
C | ARG39 |
C | GLU90 |
C | GLN127 |
C | ASP131 |
D | ASP276 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue EDO D 501 |
Chain | Residue |
B | PGE505 |
D | ARG258 |
D | GLN344 |
D | SER345 |
D | VAL346 |
D | GLY348 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue EDO D 502 |
Chain | Residue |
D | VAL27 |
D | HIS28 |
D | ARG32 |
D | GLU34 |
D | EDO503 |
site_id | AE5 |
Number of Residues | 1 |
Details | binding site for residue EDO D 503 |
Chain | Residue |
D | EDO502 |
site_id | AE6 |
Number of Residues | 2 |
Details | binding site for residue EDO D 504 |
Chain | Residue |
D | ASP157 |
D | ASP160 |
site_id | AE7 |
Number of Residues | 1 |
Details | binding site for residue EDO D 505 |
Chain | Residue |
D | ASP11 |
site_id | AE8 |
Number of Residues | 5 |
Details | binding site for residue EDO D 507 |
Chain | Residue |
D | GLU167 |
D | TYR298 |
D | GLU356 |
D | GLU409 |
D | HOH604 |
site_id | AE9 |
Number of Residues | 4 |
Details | binding site for residue EDO D 508 |
Chain | Residue |
C | ASP276 |
D | GLU90 |
D | GLN127 |
D | ASP131 |
site_id | AF1 |
Number of Residues | 2 |
Details | binding site for residue EDO D 509 |
Chain | Residue |
D | GLU107 |
D | ARG154 |
site_id | AF2 |
Number of Residues | 2 |
Details | binding site for residue EDO D 510 |
Chain | Residue |
D | HIS181 |
D | ALA411 |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LYITENGAA |
Chain | Residue | Details |
A | LEU352-ALA360 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlFGtAtASYQiEgA |
Chain | Residue | Details |
A | PHE12-ALA26 |