2J4G
Bacteroides thetaiotaomicron GH84 O-GlcNAcase in complex with n-butyl- thiazoline inhibitor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006517 | biological_process | protein deglycosylation |
A | 0015929 | molecular_function | hexosaminidase activity |
A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0042802 | molecular_function | identical protein binding |
A | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
A | 1901135 | biological_process | carbohydrate derivative metabolic process |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006517 | biological_process | protein deglycosylation |
B | 0015929 | molecular_function | hexosaminidase activity |
B | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0042802 | molecular_function | identical protein binding |
B | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACT A1591 |
Chain | Residue |
A | LYS562 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B1591 |
Chain | Residue |
A | ASN288 |
A | ASN290 |
B | ASP243 |
B | HIS433 |
B | NB11590 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NB1 A1590 |
Chain | Residue |
A | LYS166 |
A | ASP242 |
A | ASP243 |
A | CYS278 |
A | TYR282 |
A | THR310 |
A | TRP337 |
A | ASN339 |
A | ASP344 |
A | TYR345 |
A | ASN372 |
A | GLY135 |
A | PHE136 |
A | TYR137 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NB1 B1590 |
Chain | Residue |
B | GLY135 |
B | PHE136 |
B | TYR137 |
B | LYS166 |
B | ASP242 |
B | ASP243 |
B | CYS278 |
B | TYR282 |
B | THR310 |
B | TRP337 |
B | ASN339 |
B | ASP344 |
B | TYR345 |
B | ASN372 |
B | ACT1591 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A1719 |
Chain | Residue |
A | TYR137 |
A | ASP344 |
A | TYR345 |
A | ARG347 |
A | GLN551 |
B | ASN290 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B1719 |
Chain | Residue |
A | ASN290 |
B | TYR137 |
B | ASP344 |
B | TYR345 |
B | ARG347 |
B | GLN551 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000269|PubMed:16565725 |
Chain | Residue | Details |
A | ASP243 | |
B | ASP243 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16565725 |
Chain | Residue | Details |
A | GLY135 | |
B | ASP242 | |
B | TYR282 | |
B | TRP337 | |
B | ASP344 | |
B | ASN372 | |
A | LYS166 | |
A | ASP242 | |
A | TYR282 | |
A | TRP337 | |
A | ASP344 | |
A | ASN372 | |
B | GLY135 | |
B | LYS166 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qba |
Chain | Residue | Details |
A | ARG313 | |
A | ASP312 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qba |
Chain | Residue | Details |
B | ARG313 | |
B | ASP312 |