8VL7
Co-crystal structure of human TREX1 in complex with an inhibitor
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0008408 | molecular_function | 3'-5' exonuclease activity |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0008408 | molecular_function | 3'-5' exonuclease activity |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0008408 | molecular_function | 3'-5' exonuclease activity |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0008408 | molecular_function | 3'-5' exonuclease activity |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0008408 | molecular_function | 3'-5' exonuclease activity |
| F | 0003676 | molecular_function | nucleic acid binding |
| F | 0008408 | molecular_function | 3'-5' exonuclease activity |
| G | 0003676 | molecular_function | nucleic acid binding |
| G | 0008408 | molecular_function | 3'-5' exonuclease activity |
| H | 0003676 | molecular_function | nucleic acid binding |
| H | 0008408 | molecular_function | 3'-5' exonuclease activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q91XB0 |
| Chain | Residue | Details |
| A | HIS195 | |
| B | HIS195 | |
| C | HIS195 | |
| D | HIS195 | |
| E | HIS195 | |
| F | HIS195 | |
| G | HIS195 | |
| H | HIS195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q91XB0 |
| Chain | Residue | Details |
| A | ASP18 | |
| C | GLU20 | |
| C | TYR129 | |
| C | ASP200 | |
| D | ASP18 | |
| D | GLU20 | |
| D | TYR129 | |
| D | ASP200 | |
| E | ASP18 | |
| E | GLU20 | |
| E | TYR129 | |
| A | GLU20 | |
| E | ASP200 | |
| F | ASP18 | |
| F | GLU20 | |
| F | TYR129 | |
| F | ASP200 | |
| G | ASP18 | |
| G | GLU20 | |
| G | TYR129 | |
| G | ASP200 | |
| H | ASP18 | |
| A | TYR129 | |
| H | GLU20 | |
| H | TYR129 | |
| H | ASP200 | |
| A | ASP200 | |
| B | ASP18 | |
| B | GLU20 | |
| B | TYR129 | |
| B | ASP200 | |
| C | ASP18 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | SER78 | |
| B | SER78 | |
| C | SER78 | |
| D | SER78 | |
| E | SER78 | |
| F | SER78 | |
| G | SER78 | |
| H | SER78 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER167 | |
| B | SER167 | |
| C | SER167 | |
| D | SER167 | |
| E | SER167 | |
| F | SER167 | |
| G | SER167 | |
| H | SER167 |
