3LPO
Crystal structure of the N-terminal domain of sucrase-isomaltase
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 |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0030246 | molecular_function | carbohydrate binding |
Functional Information from PROSITE/UniProt
| site_id | PS00025 |
| Number of Residues | 22 |
| Details | P_TREFOIL_1 P-type 'Trefoil' domain signature. RinCiPeqfpTegiCaqrgCCW |
| Chain | Residue | Details |
| A | ARG41-TRP62 |
| site_id | PS00129 |
| Number of Residues | 8 |
| Details | GLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. GLWiDMNE |
| Chain | Residue | Details |
| A | GLY468-GLU475 |
| site_id | PS00707 |
| Number of Residues | 31 |
| Details | GLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GADICGFvaeTteeLCrRWmqLGAFyPFsRN |
| Chain | Residue | Details |
| A | GLY598-ASN628 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile; for isomaltase activity => ECO:0000255|PROSITE-ProRule:PRU10066, ECO:0000269|PubMed:20356844 |
| Chain | Residue | Details |
| A | ASP472 | |
| B | ASP472 | |
| C | ASP472 | |
| D | ASP472 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: For isomaltase activity => ECO:0000269|PubMed:20356844 |
| Chain | Residue | Details |
| A | ASP571 | |
| B | ASP571 | |
| C | ASP571 | |
| D | ASP571 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP231 | |
| C | ASP355 | |
| C | ARG555 | |
| C | HIS629 | |
| D | ASP231 | |
| D | ASP355 | |
| D | ARG555 | |
| D | HIS629 | |
| A | ASP355 | |
| A | ARG555 | |
| A | HIS629 | |
| B | ASP231 | |
| B | ASP355 | |
| B | ARG555 | |
| B | HIS629 | |
| C | ASP231 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | MOD_RES: Sulfotyrosine => ECO:0000255 |
| Chain | Residue | Details |
| A | TYR204 | |
| B | TYR358 | |
| B | TYR367 | |
| B | TYR634 | |
| B | TYR730 | |
| B | TYR732 | |
| C | TYR204 | |
| C | TYR206 | |
| C | TYR358 | |
| C | TYR367 | |
| C | TYR634 | |
| A | TYR206 | |
| C | TYR730 | |
| C | TYR732 | |
| D | TYR204 | |
| D | TYR206 | |
| D | TYR358 | |
| D | TYR367 | |
| D | TYR634 | |
| D | TYR730 | |
| D | TYR732 | |
| A | TYR358 | |
| A | TYR367 | |
| A | TYR634 | |
| A | TYR730 | |
| A | TYR732 | |
| B | TYR204 | |
| B | TYR206 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20356844 |
| Chain | Residue | Details |
| A | ASN66 | |
| C | ASN422 | |
| C | ASN822 | |
| C | ASN871 | |
| D | ASN66 | |
| D | ASN422 | |
| D | ASN822 | |
| D | ASN871 | |
| A | ASN422 | |
| A | ASN822 | |
| A | ASN871 | |
| B | ASN66 | |
| B | ASN422 | |
| B | ASN822 | |
| B | ASN871 | |
| C | ASN66 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN404 | |
| D | ASN404 | |
| D | ASN790 | |
| D | ASN893 | |
| A | ASN790 | |
| A | ASN893 | |
| B | ASN404 | |
| B | ASN790 | |
| B | ASN893 | |
| C | ASN404 | |
| C | ASN790 | |
| C | ASN893 |
