1UKO
Crystal structure of soybean beta-amylase mutant substituted at surface region
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0005983 | biological_process | starch catabolic process |
| A | 0016161 | molecular_function | beta-amylase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0005983 | biological_process | starch catabolic process |
| B | 0016161 | molecular_function | beta-amylase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0000272 | biological_process | polysaccharide catabolic process |
| C | 0005983 | biological_process | starch catabolic process |
| C | 0016161 | molecular_function | beta-amylase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0000272 | biological_process | polysaccharide catabolic process |
| D | 0005983 | biological_process | starch catabolic process |
| D | 0016161 | molecular_function | beta-amylase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3000 |
| Chain | Residue |
| A | TYR67 |
| A | SER160 |
| A | ASN164 |
| A | HOH1773 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3001 |
| Chain | Residue |
| A | ARG347 |
| A | SER349 |
| A | HOH701 |
| A | HOH1822 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3002 |
| Chain | Residue |
| A | ARG376 |
| A | HOH1871 |
| A | HIS336 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3003 |
| Chain | Residue |
| A | LYS291 |
| A | ARG376 |
| A | PHE414 |
| A | ASN455 |
| A | HIS456 |
| A | ALA457 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3004 |
| Chain | Residue |
| B | TYR67 |
| B | SER160 |
| B | ASN164 |
| B | HOH1959 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3005 |
| Chain | Residue |
| B | ARG347 |
| B | SER349 |
| B | HOH1722 |
| B | HOH1726 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3006 |
| Chain | Residue |
| B | HIS336 |
| B | ARG376 |
| B | HOH1173 |
| B | HOH1180 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3007 |
| Chain | Residue |
| B | LYS291 |
| B | ARG376 |
| B | PHE414 |
| B | ASN455 |
| B | HIS456 |
| B | ALA457 |
| B | HOH1325 |
| B | HOH1704 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3008 |
| Chain | Residue |
| C | TYR67 |
| C | SER160 |
| C | ASN164 |
| C | HOH1205 |
| C | HOH1530 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3009 |
| Chain | Residue |
| C | ARG347 |
| C | SER349 |
| C | HOH1266 |
| C | HOH1588 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3010 |
| Chain | Residue |
| C | HIS336 |
| C | ARG376 |
| C | HOH1263 |
| C | HOH1584 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3011 |
| Chain | Residue |
| C | LYS291 |
| C | ARG376 |
| C | PHE414 |
| C | ASN455 |
| C | ALA457 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3012 |
| Chain | Residue |
| D | TYR67 |
| D | SER160 |
| D | ASN164 |
| D | HOH1318 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3013 |
| Chain | Residue |
| D | ARG347 |
| D | SER349 |
| D | HOH971 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3014 |
| Chain | Residue |
| D | HIS336 |
| D | ARG376 |
| D | HOH969 |
| D | HOH1346 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3015 |
| Chain | Residue |
| B | HOH1154 |
| D | LYS291 |
| D | ARG376 |
| D | PHE414 |
| D | ASN455 |
| D | ALA457 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3016 |
| Chain | Residue |
| A | ARG70 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3017 |
| Chain | Residue |
| B | ARG70 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3018 |
| Chain | Residue |
| C | ARG70 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3019 |
| Chain | Residue |
| D | ARG70 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3020 |
| Chain | Residue |
| A | ASN98 |
| A | PRO193 |
| A | GLN194 |
| A | HOH675 |
| A | HOH1794 |
| A | HOH1855 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3021 |
| Chain | Residue |
| B | ASN98 |
| B | TYR192 |
| B | PRO193 |
| B | GLN194 |
| B | HOH1148 |
| B | HOH1638 |
| B | HOH1639 |
| B | HOH1656 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3022 |
| Chain | Residue |
| C | ASN98 |
| C | PRO193 |
| C | GLN194 |
| C | HOH1405 |
| C | HOH1406 |
| C | HOH1407 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3023 |
| Chain | Residue |
| D | HOH1298 |
| D | HOH1307 |
| D | HOH1319 |
| D | ASN98 |
| D | PRO193 |
| D | GLN194 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2474529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8011643","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8174545","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8011643","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bya |
| Chain | Residue | Details |
| A | GLU186 | |
| A | ASP101 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bya |
| Chain | Residue | Details |
| B | GLU186 | |
| B | ASP101 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bya |
| Chain | Residue | Details |
| C | GLU186 | |
| C | ASP101 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bya |
| Chain | Residue | Details |
| D | GLU186 | |
| D | ASP101 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 436 |
| Chain | Residue | Details |
| A | ASP101 | electrostatic stabiliser |
| A | GLU186 | proton shuttle (general acid/base) |
| A | THR342 | electrostatic stabiliser |
| A | GLU380 | proton shuttle (general acid/base) |
| A | LEU383 | steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 436 |
| Chain | Residue | Details |
| B | ASP101 | electrostatic stabiliser |
| B | GLU186 | proton shuttle (general acid/base) |
| B | THR342 | electrostatic stabiliser |
| B | GLU380 | proton shuttle (general acid/base) |
| B | LEU383 | steric role |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 436 |
| Chain | Residue | Details |
| C | ASP101 | electrostatic stabiliser |
| C | GLU186 | proton shuttle (general acid/base) |
| C | THR342 | electrostatic stabiliser |
| C | GLU380 | proton shuttle (general acid/base) |
| C | LEU383 | steric role |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 436 |
| Chain | Residue | Details |
| D | ASP101 | electrostatic stabiliser |
| D | GLU186 | proton shuttle (general acid/base) |
| D | THR342 | electrostatic stabiliser |
| D | GLU380 | proton shuttle (general acid/base) |
| D | LEU383 | steric role |






