1MQP
THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE FROM BACILLUS STEAROTHERMOPHILUS T-6
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0033939 | molecular_function | xylan alpha-1,2-glucuronosidase activity |
| A | 0045493 | biological_process | xylan catabolic process |
| A | 0046559 | molecular_function | alpha-glucuronidase activity |
| A | 2000886 | biological_process | glucuronoxylan catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 701 |
| Chain | Residue |
| A | TYR91 |
| A | HOH884 |
| A | HOH930 |
| A | TYR116 |
| A | HIS120 |
| A | ARG123 |
| A | SER189 |
| A | VAL190 |
| A | GLY191 |
| A | ARG467 |
| A | TRP470 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 702 |
| Chain | Residue |
| A | ARG368 |
| A | GLU369 |
| A | VAL371 |
| A | GLU409 |
| A | PHE413 |
| A | LEU585 |
| A | HOH809 |
| A | HOH848 |
| A | HOH983 |
| A | HOH1038 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 703 |
| Chain | Residue |
| A | LYS620 |
| A | LYS653 |
| A | ARG656 |
| A | HOH1011 |
| A | HOH1193 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 704 |
| Chain | Residue |
| A | SER19 |
| A | GLU129 |
| A | HIS599 |
| A | HOH890 |
| A | HOH918 |
| A | HOH1215 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 705 |
| Chain | Residue |
| A | TYR340 |
| A | ALA377 |
| A | ALA565 |
| A | GLN566 |
| A | TYR567 |
| A | PHE568 |
| A | PRO569 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 706 |
| Chain | Residue |
| A | ARG335 |
| A | HIS527 |
| A | TYR535 |
| A | TRP540 |
| A | HOH971 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 707 |
| Chain | Residue |
| A | GLU570 |
| A | MET574 |
| A | THR580 |
| A | HOH1218 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:14573597 |
| Chain | Residue | Details |
| A | GLU285 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:14573597 |
| Chain | Residue | Details |
| A | ASP364 | |
| A | GLU392 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS281 | |
| A | ARG318 | |
| A | ARG335 | |
| A | LYS359 | |
| A | GLU158 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN201 | |
| A | GLU386 | |
| A | GLU510 | |
| A | TRP540 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA => ECO:0000250 |
| Chain | Residue | Details |
| A | TRP150 | |
| A | TRP540 |
