8RW3
Crystal Structure of Agd31B, alpha-transglucosylase, complexed with a non-covalent 1,2- Cyclophellitol aziridine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0030246 | molecular_function | carbohydrate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0030246 | molecular_function | carbohydrate binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0030246 | molecular_function | carbohydrate binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:23132856 |
Chain | Residue | Details |
C | ASP412 | |
A | ASP412 | |
B | ASP412 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P31434 |
Chain | Residue | Details |
C | GLU415 | |
A | GLU415 | |
B | GLU415 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P31434 |
Chain | Residue | Details |
C | ASP480 | |
A | ASP480 | |
B | ASP480 |
site_id | SWS_FT_FI4 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23132856 |
Chain | Residue | Details |
C | ASP299 | |
A | HIS540 | |
B | ASP299 | |
B | GLU417 | |
B | ARG463 | |
B | ASP480 | |
B | HIS540 | |
C | GLU417 | |
C | ARG463 | |
C | ASP480 | |
C | HIS540 | |
A | ASP299 | |
A | GLU417 | |
A | ARG463 | |
A | ASP480 |