4XEO
Crystal Structure of human AlaRS catalytic domain with R329H mutation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004813 | molecular_function | alanine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006419 | biological_process | alanyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004813 | molecular_function | alanine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006419 | biological_process | alanyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue A5A A 501 |
| Chain | Residue |
| A | ALA44 |
| A | ILE214 |
| A | ASN216 |
| A | VAL218 |
| A | ASP239 |
| A | THR240 |
| A | GLY241 |
| A | GLY243 |
| A | ARG246 |
| A | HOH689 |
| A | HOH695 |
| A | ARG77 |
| A | TYR93 |
| A | HIS94 |
| A | HIS95 |
| A | PHE98 |
| A | MET100 |
| A | TRP176 |
| A | GLU213 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | HIS27 |
| A | SER28 |
| A | SER29 |
| A | ALA30 |
| A | LYS74 |
| A | GLU363 |
| A | HOH721 |
| A | HOH736 |
| A | HOH831 |
| A | HOH867 |
| B | GLU268 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLN12 |
| A | ILE15 |
| A | LYS19 |
| A | HOH826 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | TYR109 |
| A | PHE110 |
| A | GLU112 |
| A | LEU113 |
| A | HOH763 |
| A | HOH845 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | ASP86 |
| A | ARG330 |
| A | ARG333 |
| A | TYR334 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 506 |
| Chain | Residue |
| A | GLU189 |
| A | GLU213 |
| A | HOH784 |
| A | HOH820 |
| A | HOH863 |
| A | HOH1016 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue A5A B 501 |
| Chain | Residue |
| B | ALA44 |
| B | ARG77 |
| B | TYR93 |
| B | HIS94 |
| B | HIS95 |
| B | PHE98 |
| B | MET100 |
| B | TRP176 |
| B | GLU213 |
| B | ILE214 |
| B | ASN216 |
| B | VAL218 |
| B | ASP239 |
| B | THR240 |
| B | GLY241 |
| B | GLY243 |
| B | ARG246 |
| B | HOH651 |
| B | HOH653 |
| B | HOH747 |
| B | HOH893 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | GLN12 |
| B | ILE15 |
| B | LYS19 |
| B | HOH605 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| A | GLU268 |
| B | HIS27 |
| B | SER28 |
| B | SER29 |
| B | ALA30 |
| B | LYS74 |
| B | GLU363 |
| B | HOH601 |
| B | HOH608 |
| B | HOH610 |
| B | HOH614 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | ASP86 |
| B | ARG330 |
| B | ARG333 |
| B | TYR334 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 505 |
| Chain | Residue |
| B | TYR109 |
| B | PHE110 |
| B | GLU112 |
| B | LEU113 |
| B | HOH713 |
| B | HOH968 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 506 |
| Chain | Residue |
| B | HOH771 |
| B | HOH976 |
| B | HOH977 |
| B | GLU189 |
| B | GLU213 |
| B | HOH714 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27622773","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of wild type human AlaRS catalytic domain.","authors":["Zhou H.","Yang X.L."]}},{"source":"PDB","id":"4XEM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XEO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KNN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
