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 | 0008378 | molecular_function | galactosyltransferase activity |
| A | 0016787 | molecular_function | hydrolase 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 | 0008378 | molecular_function | galactosyltransferase activity |
| B | 0016787 | molecular_function | hydrolase 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 | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Site: {"description":"Not N6-methylated"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-methyllysine; partial","evidences":[{"source":"PubMed","id":"14660666","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"14660666","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
