4FNP
Crystal structure of GH36 alpha-galactosidase AgaA A355E from Geobacillus stearothermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004557 | molecular_function | alpha-galactosidase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0033531 | biological_process | stachyose metabolic process |
| A | 0034484 | biological_process | raffinose catabolic process |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004557 | molecular_function | alpha-galactosidase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0033531 | biological_process | stachyose metabolic process |
| B | 0034484 | biological_process | raffinose catabolic process |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004557 | molecular_function | alpha-galactosidase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0033531 | biological_process | stachyose metabolic process |
| C | 0034484 | biological_process | raffinose catabolic process |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004557 | molecular_function | alpha-galactosidase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0033531 | biological_process | stachyose metabolic process |
| D | 0034484 | biological_process | raffinose catabolic process |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 801 |
| Chain | Residue |
| A | ALA670 |
| A | GLU671 |
| A | ALA672 |
| C | GLY200 |
| C | ARG201 |
| C | TRP204 |
| C | ASN549 |
| C | SER554 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 802 |
| Chain | Residue |
| A | GLY138 |
| A | ASP139 |
| A | ALA140 |
| A | GLY143 |
| A | LEU144 |
| A | GLU145 |
| A | LYS105 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 803 |
| Chain | Residue |
| A | PHE12 |
| A | HIS13 |
| A | LEU14 |
| A | ILE109 |
| A | LEU133 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 801 |
| Chain | Residue |
| B | GLY200 |
| B | ARG201 |
| B | TRP204 |
| B | ASN549 |
| B | SER554 |
| B | VAL583 |
| D | GLU671 |
| D | ALA672 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 802 |
| Chain | Residue |
| B | LYS105 |
| B | GLY138 |
| B | ASP139 |
| B | ALA140 |
| B | GLY143 |
| B | LEU144 |
| B | GLU145 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 803 |
| Chain | Residue |
| B | PHE12 |
| B | HIS13 |
| B | LEU14 |
| B | ILE109 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 801 |
| Chain | Residue |
| A | GLY200 |
| A | ARG201 |
| A | TRP204 |
| A | ASN549 |
| A | SER554 |
| C | ALA670 |
| C | GLU671 |
| C | ALA672 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 802 |
| Chain | Residue |
| C | LYS105 |
| C | GLY138 |
| C | ASP139 |
| C | GLY143 |
| C | LEU144 |
| C | GLU145 |
| C | LYS168 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 803 |
| Chain | Residue |
| C | PHE12 |
| C | HIS13 |
| C | LEU14 |
| C | ILE109 |
| C | LEU133 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 801 |
| Chain | Residue |
| B | GLU671 |
| B | ALA672 |
| D | GLY200 |
| D | ARG201 |
| D | ASN549 |
| D | SER554 |
| D | VAL583 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 802 |
| Chain | Residue |
| D | LYS105 |
| D | GLY138 |
| D | ASP139 |
| D | GLY143 |
| D | LEU144 |
| D | GLU145 |
| D | LYS168 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 803 |
| Chain | Residue |
| D | PHE12 |
| D | HIS13 |
| D | LEU14 |
Functional Information from PROSITE/UniProt
| site_id | PS00512 |
| Number of Residues | 16 |
| Details | ALPHA_GALACTOSIDASE Alpha-galactosidase signature. GIelVvLDDg.Wfge....RD |
| Chain | Residue | Details |
| A | GLY359-ASP374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:23012371 |
| Chain | Residue | Details |
| A | ASP478 | |
| B | ASP478 | |
| C | ASP478 | |
| D | ASP478 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:23012371 |
| Chain | Residue | Details |
| A | ASP548 | |
| B | ASP548 | |
| C | ASP548 | |
| D | ASP548 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23012371, ECO:0007744|PDB:4FNT |
| Chain | Residue | Details |
| A | ASP53 | |
| B | ASP366 | |
| B | ARG443 | |
| B | LYS476 | |
| B | CYS526 | |
| B | ASP548 | |
| C | ASP53 | |
| C | TRP199 | |
| C | ASP366 | |
| C | ARG443 | |
| C | LYS476 | |
| A | TRP199 | |
| C | CYS526 | |
| C | ASP548 | |
| D | ASP53 | |
| D | TRP199 | |
| D | ASP366 | |
| D | ARG443 | |
| D | LYS476 | |
| D | CYS526 | |
| D | ASP548 | |
| A | ASP366 | |
| A | ARG443 | |
| A | LYS476 | |
| A | CYS526 | |
| A | ASP548 | |
| B | ASP53 | |
| B | TRP199 |
