6Y7B
X-ray structure of the Haloalkane dehalogenase HaloTag7 labeled with a chloroalkane-carbopyronine fluorophore substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018786 | molecular_function | haloalkane dehalogenase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018786 | molecular_function | haloalkane dehalogenase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0009636 | biological_process | response to toxic substance |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0018786 | molecular_function | haloalkane dehalogenase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0009636 | biological_process | response to toxic substance |
| D | 0016020 | cellular_component | membrane |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0018786 | molecular_function | haloalkane dehalogenase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0009636 | biological_process | response to toxic substance |
| E | 0016020 | cellular_component | membrane |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0018786 | molecular_function | haloalkane dehalogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue OEK A 301 |
| Chain | Residue |
| A | ASP106 |
| A | ALA145 |
| A | THR148 |
| A | PHE149 |
| A | GLN165 |
| A | GLY171 |
| A | THR172 |
| A | MET175 |
| A | ASN272 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ASN41 |
| A | TRP107 |
| A | PHE205 |
| A | PRO206 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ASN41 |
| B | TRP107 |
| B | PRO206 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 302 |
| Chain | Residue |
| C | ASN41 |
| C | TRP107 |
| C | OEK301 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| D | ASN41 |
| D | TRP107 |
| D | PRO206 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL E 302 |
| Chain | Residue |
| E | TRP107 |
| E | PHE205 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide OEK B 301 and ASP B 106 |
| Chain | Residue |
| B | GLY40 |
| B | ASN41 |
| B | HIS105 |
| B | TRP107 |
| B | GLY108 |
| B | SER109 |
| B | ALA110 |
| B | GLU130 |
| B | ILE132 |
| B | THR148 |
| B | GLN165 |
| B | GLU170 |
| B | GLY171 |
| B | THR172 |
| B | MET175 |
| B | ASN272 |
| E | THR58 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide OEK C 301 and ASP C 106 |
| Chain | Residue |
| C | ASN41 |
| C | HIS105 |
| C | TRP107 |
| C | GLY108 |
| C | SER109 |
| C | ALA110 |
| C | GLU130 |
| C | ILE132 |
| C | ALA145 |
| C | THR148 |
| C | PHE149 |
| C | GLN165 |
| C | GLU170 |
| C | THR172 |
| C | MET175 |
| C | LEU246 |
| C | ASN272 |
| C | CL302 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide OEK D 301 and ASP D 106 |
| Chain | Residue |
| C | THR137 |
| C | TRP138 |
| C | ASP139 |
| C | GLN150 |
| C | ALA212 |
| D | ASN41 |
| D | HIS105 |
| D | TRP107 |
| D | GLY108 |
| D | SER109 |
| D | ALA110 |
| D | GLU130 |
| D | ILE132 |
| D | PHE144 |
| D | ALA145 |
| D | THR148 |
| D | GLN165 |
| D | VAL167 |
| D | GLU170 |
| D | GLY171 |
| D | THR172 |
| D | LEU246 |
| D | ASN272 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide OEK E 301 and ASP E 106 |
| Chain | Residue |
| E | ASN41 |
| E | HIS105 |
| E | TRP107 |
| E | GLY108 |
| E | SER109 |
| E | ALA110 |
| E | GLU130 |
| E | ILE132 |
| E | PHE144 |
| E | ALA145 |
| E | THR148 |
| E | PHE149 |
| E | GLN165 |
| E | THR172 |
| E | ASN272 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 620 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
