1O4Z
THE THREE-DIMENSIONAL STRUCTURE OF BETA-AGARASE B FROM ZOBELLIA GALACTANIVORANS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0033916 | molecular_function | beta-agarase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0033916 | molecular_function | beta-agarase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0009279 | cellular_component | cell outer membrane |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0033916 | molecular_function | beta-agarase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0009279 | cellular_component | cell outer membrane |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0033916 | molecular_function | beta-agarase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 1001 |
| Chain | Residue |
| B | VAL239 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 1002 |
| Chain | Residue |
| C | GLU197 |
| C | SER198 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 1003 |
| Chain | Residue |
| D | ASN83 |
| D | GLU85 |
| D | GLY127 |
| D | ASP343 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1004 |
| Chain | Residue |
| A | GLY127 |
| A | ASP343 |
| A | HOH2119 |
| A | ASN83 |
| A | GLU85 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 1005 |
| Chain | Residue |
| B | ASN83 |
| B | GLU85 |
| B | GLY127 |
| B | ASP343 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 1006 |
| Chain | Residue |
| C | ASN83 |
| C | GLY127 |
| C | ASP343 |
| C | HOH2198 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA A 1007 |
| Chain | Residue |
| A | ARG246 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 1008 |
| Chain | Residue |
| B | GLU128 |
| B | HOH2232 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA C 1009 |
| Chain | Residue |
| C | LYS118 |
| C | ARG119 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EPE C 2001 |
| Chain | Residue |
| C | PRO112 |
| C | ASP173 |
| C | TRP175 |
| C | GLU184 |
| C | ASP186 |
| C | GLU189 |
| C | GLU308 |
| C | GLN310 |
| C | THR311 |
| C | TRP312 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EPE A 2002 |
| Chain | Residue |
| A | PRO112 |
| A | ASP173 |
| A | TRP175 |
| A | GLU184 |
| A | ASP186 |
| A | GLU189 |
| A | GLU308 |
| A | GLN310 |
| A | THR311 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EPE D 2003 |
| Chain | Residue |
| D | TRP175 |
| D | GLU184 |
| D | ASP186 |
| D | GLU189 |
| D | GLU308 |
| D | GLN310 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EPE B 2004 |
| Chain | Residue |
| B | PRO112 |
| B | TRP175 |
| B | GLU184 |
| B | ASP186 |
| B | GLU189 |
| B | GLU308 |
| B | GLN310 |
| B | THR311 |
| B | HOH2084 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:G0L322 |
| Chain | Residue | Details |
| A | GLU184 | |
| B | GLU184 | |
| C | GLU184 | |
| D | GLU184 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:G0L322 |
| Chain | Residue | Details |
| A | GLU189 | |
| B | GLU189 | |
| C | GLU189 | |
| D | GLU189 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22778272 |
| Chain | Residue | Details |
| A | TYR105 | |
| B | HIS215 | |
| B | ARG219 | |
| B | ASP224 | |
| B | GLN226 | |
| B | GLU308 | |
| C | TYR105 | |
| C | ASP181 | |
| C | HIS215 | |
| C | ARG219 | |
| C | ASP224 | |
| A | ASP181 | |
| C | GLN226 | |
| C | GLU308 | |
| D | TYR105 | |
| D | ASP181 | |
| D | HIS215 | |
| D | ARG219 | |
| D | ASP224 | |
| D | GLN226 | |
| D | GLU308 | |
| A | HIS215 | |
| A | ARG219 | |
| A | ASP224 | |
| A | GLN226 | |
| A | GLU308 | |
| B | TYR105 | |
| B | ASP181 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2ayh |
| Chain | Residue | Details |
| A | ASP186 | |
| A | GLU197 | |
| A | GLU184 |
