3HXV
Crystal Structure of catalytic fragment of E. coli AlaRS in complex with GlySA
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EPE A 442 |
| Chain | Residue |
| A | SER25 |
| A | HOH915 |
| A | HOH931 |
| A | ARG66 |
| A | GLU125 |
| A | ARG152 |
| A | GLU346 |
| A | ASP347 |
| A | HOH491 |
| A | HOH739 |
| A | HOH912 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HED A 443 |
| Chain | Residue |
| A | ARG60 |
| A | ASP100 |
| A | TYR101 |
| A | PHE109 |
| A | ARG396 |
| A | ARG434 |
| A | HOH839 |
| A | HOH881 |
| A | HOH889 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE G5A A 444 |
| Chain | Residue |
| A | ALA41 |
| A | ARG69 |
| A | ASP76 |
| A | ARG85 |
| A | HIS86 |
| A | HIS87 |
| A | PHE90 |
| A | MET92 |
| A | TRP170 |
| A | GLU183 |
| A | GLU209 |
| A | ILE210 |
| A | ASN212 |
| A | ASP235 |
| A | GLY237 |
| A | GLY239 |
| A | ARG242 |
| A | HOH599 |
| A | HOH618 |
| A | HOH740 |
| A | HOH892 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BME A 445 |
| Chain | Residue |
| A | SER1 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HED A 446 |
| Chain | Residue |
| A | PRO34 |
| A | ARG305 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HED A 447 |
| Chain | Residue |
| A | PHE120 |
| A | TYR186 |
| A | VAL246 |
| A | LEU247 |
| A | HIS249 |
| A | HOH544 |
| A | HOH584 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30274179","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
