6N6J
Human REXO2 bound to pAA
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ASN110 |
| D | A604 |
| A | LYS158 |
| A | ALA160 |
| A | HIS162 |
| A | ASP167 |
| A | HOH426 |
| A | HOH476 |
| A | HOH556 |
| D | A603 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MLI A 302 |
| Chain | Residue |
| A | LYS186 |
| A | ILE187 |
| A | HOH409 |
| B | ARG97 |
| B | PRO102 |
| B | GLU151 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 701 |
| Chain | Residue |
| A | ASP15 |
| A | HOH476 |
| A | HOH507 |
| D | A603 |
| D | A604 |
| D | HOH802 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| A | GLN86 |
| A | GLU89 |
| A | PRO124 |
| A | GLN125 |
| B | GLU45 |
| B | SER169 |
| B | HOH424 |
| B | HOH443 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 701 |
| Chain | Residue |
| B | ASN110 |
| B | ASP167 |
| C | A603 |
| C | A604 |
| C | HOH805 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 702 |
| Chain | Residue |
| B | ASP15 |
| B | HOH472 |
| C | A603 |
| C | A604 |
| C | HOH802 |
| C | HOH805 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022 |
| Chain | Residue | Details |
| A | ILE194 | |
| B | ILE194 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, ECO:0007744|PDB:6RCN |
| Chain | Residue | Details |
| A | PRO47 | |
| A | LEU49 | |
| B | PRO47 | |
| B | LEU49 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6RCN |
| Chain | Residue | Details |
| A | TRP147 | |
| B | TRP147 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30926754, ECO:0007744|PDB:6J7Y |
| Chain | Residue | Details |
| A | GLU199 | |
| B | GLU199 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | SITE: Important for dinucleotide binding => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:32365187 |
| Chain | Residue | Details |
| A | GLN53 | |
| A | VAL96 | |
| A | ALA164 | |
| B | GLN53 | |
| B | VAL96 | |
| B | ALA164 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | PHE92 | |
| B | PHE92 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | TYR122 | |
| B | TYR122 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D8S4 |
| Chain | Residue | Details |
| A | LYS173 | |
| B | LYS173 |
