4KC8
Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031222 | biological_process | arabinan catabolic process |
| A | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031222 | biological_process | arabinan catabolic process |
| B | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0031222 | biological_process | arabinan catabolic process |
| C | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS A 501 |
| Chain | Residue |
| A | ASP32 |
| A | LEU169 |
| A | ASP170 |
| A | GLU223 |
| A | LEU245 |
| A | HIS314 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 502 |
| Chain | Residue |
| A | ALA96 |
| A | ASP170 |
| A | PRO171 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 501 |
| Chain | Residue |
| B | HIS31 |
| B | ASP32 |
| B | TRP95 |
| B | LEU169 |
| B | ASP170 |
| B | GLU223 |
| B | LEU245 |
| B | HIS314 |
| B | HOH603 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | PRO171 |
| B | HIS314 |
| B | HOH645 |
| B | HOH906 |
| B | HOH907 |
| B | HOH908 |
| B | HOH910 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 501 |
| Chain | Residue |
| C | HIS314 |
| C | HOH705 |
| C | HOH706 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24469445 |
| Chain | Residue | Details |
| A | ASP32 | |
| B | ASP32 | |
| C | ASP32 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:24469445 |
| Chain | Residue | Details |
| A | GLU223 | |
| B | GLU223 | |
| C | GLU223 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP32 | |
| B | HIS314 | |
| C | ASP32 | |
| C | ASN167 | |
| C | SER187 | |
| C | HIS219 | |
| C | HIS314 | |
| A | ASN167 | |
| A | SER187 | |
| A | HIS219 | |
| A | HIS314 | |
| B | ASP32 | |
| B | ASN167 | |
| B | SER187 | |
| B | HIS219 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24469445 |
| Chain | Residue | Details |
| A | GLY117 | |
| B | GLY117 | |
| C | GLY117 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Important for catalytic activity => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP170 | |
| B | ASP170 | |
| C | ASP170 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | SITE: Important for substrate recognition => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS314 | |
| B | HIS314 | |
| C | HIS314 |
