6A8I
Crystal structure of endo-arabinanase ABN-TS D147N mutant in complex with arabinohexaose
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 |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031222 | biological_process | arabinan catabolic process |
| B | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:15944411 |
| Chain | Residue | Details |
| A | ASP27 | |
| B | ASP27 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:15944411 |
| Chain | Residue | Details |
| A | GLU201 | |
| B | GLU201 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP27 | |
| A | ASN144 | |
| A | SER164 | |
| B | ASP27 | |
| B | ASN144 | |
| B | SER164 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY105 | |
| B | GLY105 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | HIS271 | |
| B | HIS271 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| 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:15944411 |
| Chain | Residue | Details |
| A | ASN147 | |
| B | ASN147 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Important for substrate recognition => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS271 | |
| B | HIS271 |
