1UKP
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 | 0016161 | molecular_function | beta-amylase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0102229 | molecular_function | amylopectin maltohydrolase activity |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0016161 | molecular_function | beta-amylase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0102229 | molecular_function | amylopectin maltohydrolase activity |
| C | 0000272 | biological_process | polysaccharide catabolic process |
| C | 0016161 | molecular_function | beta-amylase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0102229 | molecular_function | amylopectin maltohydrolase activity |
| D | 0000272 | biological_process | polysaccharide catabolic process |
| D | 0016161 | molecular_function | beta-amylase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0102229 | molecular_function | amylopectin maltohydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2000 |
| Chain | Residue |
| A | TYR67 |
| A | SER160 |
| A | ASN164 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2001 |
| Chain | Residue |
| B | SER160 |
| B | ASN164 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2002 |
| Chain | Residue |
| C | SER160 |
| C | ASN164 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 2003 |
| Chain | Residue |
| D | SER160 |
| D | ASN164 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2004 |
| Chain | Residue |
| A | ASP234 |
| A | HOH1357 |
| B | HIS146 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2005 |
| Chain | Residue |
| A | HIS146 |
| A | HOH1134 |
| B | ASP234 |
| B | GLY246 |
| B | HOH819 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2006 |
| Chain | Residue |
| C | GLY246 |
| D | HIS146 |
| D | HOH1172 |
| D | HOH1490 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2007 |
| Chain | Residue |
| C | HIS146 |
| D | ASP234 |
| D | HOH1445 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2008 |
| Chain | Residue |
| A | ARG347 |
| A | SER349 |
| A | HOH1151 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2009 |
| Chain | Residue |
| B | ARG347 |
| B | SER349 |
| B | HOH537 |
| B | HOH1425 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2010 |
| Chain | Residue |
| C | ARG347 |
| C | SER349 |
| C | HOH785 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 2011 |
| Chain | Residue |
| D | ARG347 |
| D | SER349 |
| D | HOH739 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2012 |
| Chain | Residue |
| A | LYS291 |
| A | ARG376 |
| A | PHE414 |
| A | ASN455 |
| A | HIS456 |
| A | ALA457 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2013 |
| Chain | Residue |
| B | LYS291 |
| B | ARG376 |
| B | ASN455 |
| B | HIS456 |
| B | ALA457 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2014 |
| Chain | Residue |
| C | LYS291 |
| C | ARG376 |
| C | PHE414 |
| C | ASN455 |
| C | ALA457 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 2015 |
| Chain | Residue |
| D | ARG376 |
| D | PHE414 |
| D | ASN455 |
| D | ALA457 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2016 |
| Chain | Residue |
| A | ASP387 |
| A | ALA388 |
| A | THR389 |
| A | HOH606 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2017 |
| Chain | Residue |
| B | ASP387 |
| B | ALA388 |
| B | THR389 |
| B | HOH648 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2018 |
| Chain | Residue |
| C | ASP387 |
| C | ALA388 |
| C | THR389 |
| C | HOH787 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 2019 |
| Chain | Residue |
| D | ASP387 |
| D | ALA388 |
| D | THR389 |
| D | HOH704 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10050, ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:2474529, ECO:0000269|PubMed:8011643, ECO:0000269|PubMed:8174545 |
| Chain | Residue | Details |
| A | LEU187 | |
| B | LEU187 | |
| C | LEU187 | |
| D | LEU187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:8011643 |
| Chain | Residue | Details |
| A | ASN381 | |
| B | ASN381 | |
| C | ASN381 | |
| D | ASN381 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15178253 |
| Chain | Residue | Details |
| A | VAL54 | |
| B | GLN94 | |
| B | ILE102 | |
| B | VAL296 | |
| B | TRP301 | |
| B | CYS343 | |
| B | ALA382 | |
| B | LEU421 | |
| C | VAL54 | |
| C | GLN94 | |
| C | ILE102 | |
| A | GLN94 | |
| C | VAL296 | |
| C | TRP301 | |
| C | CYS343 | |
| C | ALA382 | |
| C | LEU421 | |
| D | VAL54 | |
| D | GLN94 | |
| D | ILE102 | |
| D | VAL296 | |
| D | TRP301 | |
| A | ILE102 | |
| D | CYS343 | |
| D | ALA382 | |
| D | LEU421 | |
| A | VAL296 | |
| A | TRP301 | |
| A | CYS343 | |
| A | ALA382 | |
| A | LEU421 | |
| B | VAL54 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:2430952 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 | |
| C | THR2 | |
| D | THR2 |
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 | ILE102 | electrostatic stabiliser |
| A | LEU187 | proton shuttle (general acid/base) |
| A | CYS343 | electrostatic stabiliser |
| A | ASN381 | proton shuttle (general acid/base) |
| A | PRO384 | steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 436 |
| Chain | Residue | Details |
| B | ILE102 | electrostatic stabiliser |
| B | LEU187 | proton shuttle (general acid/base) |
| B | CYS343 | electrostatic stabiliser |
| B | ASN381 | proton shuttle (general acid/base) |
| B | PRO384 | steric role |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 436 |
| Chain | Residue | Details |
| C | ILE102 | electrostatic stabiliser |
| C | LEU187 | proton shuttle (general acid/base) |
| C | CYS343 | electrostatic stabiliser |
| C | ASN381 | proton shuttle (general acid/base) |
| C | PRO384 | steric role |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 436 |
| Chain | Residue | Details |
| D | ILE102 | electrostatic stabiliser |
| D | LEU187 | proton shuttle (general acid/base) |
| D | CYS343 | electrostatic stabiliser |
| D | ASN381 | proton shuttle (general acid/base) |
| D | PRO384 | steric role |
