3D5Z
Crystal Structure Analysis of 1,5-alpha-arabinanase catalytic mutant (AbnBE201A) complexed to arabinotriose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005737 | cellular_component | cytoplasm |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031222 | biological_process | arabinan catabolic process |
A | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:19505290 |
Chain | Residue | Details |
A | ASP27 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:19505290 |
Chain | Residue | Details |
A | ALA201 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19505290 |
Chain | Residue | Details |
A | ASP27 | |
A | GLY105 | |
A | ASN144 | |
A | SER164 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | HIS271 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:19505290 |
Chain | Residue | Details |
A | ASP147 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Important for substrate recognition => ECO:0000250 |
Chain | Residue | Details |
A | HIS271 |