4EAM
1.70A resolution structure of apo beta-glycosidase (W33G) from sulfolobus solfataricus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004565 | molecular_function | beta-galactosidase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0004565 | molecular_function | beta-galactosidase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008422 | molecular_function | beta-glucosidase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 501 |
Chain | Residue |
A | ASN264 |
A | SER265 |
A | ARG286 |
A | HOH723 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 502 |
Chain | Residue |
A | ARG440 |
A | VAL446 |
A | TYR448 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 503 |
Chain | Residue |
A | ARG295 |
A | HOH712 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD A 504 |
Chain | Residue |
A | PRO89 |
A | ASN90 |
A | TYR121 |
A | ASN123 |
A | HOH625 |
A | HOH629 |
B | THR450 |
B | HOH720 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD A 505 |
Chain | Residue |
A | GLU206 |
A | SER265 |
A | TYR322 |
A | TRS507 |
A | HOH618 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD A 506 |
Chain | Residue |
A | SER220 |
A | GLU432 |
A | TRP433 |
A | ALA434 |
A | HOH695 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRS A 507 |
Chain | Residue |
A | GLN18 |
A | GLU206 |
A | TYR322 |
A | TRP361 |
A | GLU387 |
A | TRP425 |
A | GLU432 |
A | MPD505 |
A | HOH670 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 501 |
Chain | Residue |
B | ASN264 |
B | SER265 |
B | ARG286 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 502 |
Chain | Residue |
B | ARG295 |
B | HOH768 |
B | HOH884 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 503 |
Chain | Residue |
B | ARG440 |
B | TYR448 |
B | HOH888 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD B 504 |
Chain | Residue |
B | GLU206 |
B | SER265 |
B | TYR322 |
B | TRS507 |
B | HOH617 |
B | HOH891 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MPD B 505 |
Chain | Residue |
A | PRO29 |
A | HOH757 |
B | PRO24 |
B | GLY25 |
B | TRP60 |
B | ASP125 |
B | HOH896 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD B 506 |
Chain | Residue |
B | SER220 |
B | GLU432 |
B | TRP433 |
B | ALA434 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRS B 507 |
Chain | Residue |
B | GLN18 |
B | GLU206 |
B | TYR322 |
B | TRP361 |
B | GLU387 |
B | TRP425 |
B | GLU432 |
B | MPD504 |
B | HOH695 |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MYVTENGIA |
Chain | Residue | Details |
A | MET383-ALA391 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FrFGwSqAGFQsEmG |
Chain | Residue | Details |
A | PHE8-GLY22 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255 |
Chain | Residue | Details |
A | GLU206 | |
B | GLU206 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 |
Chain | Residue | Details |
A | GLU387 | |
B | GLU387 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Not N6-methylated |
Chain | Residue | Details |
A | LYS76 | |
A | LYS102 | |
A | LYS124 | |
A | LYS138 | |
B | LYS76 | |
B | LYS102 | |
B | LYS124 | |
B | LYS138 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:14660666 |
Chain | Residue | Details |
A | LYS116 | |
A | LYS273 | |
A | LYS311 | |
B | LYS116 | |
B | LYS273 | |
B | LYS311 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:14660666 |
Chain | Residue | Details |
A | LYS135 | |
A | LYS332 | |
B | LYS135 | |
B | LYS332 |