6J7M
Complex structure of the Pseudomonas aeruginosa rhamnosyltransferase EarP with the acceptor elongation factor EF-P
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0106361 | molecular_function | protein-arginine rhamnosyltransferase activity |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0106361 | molecular_function | protein-arginine rhamnosyltransferase activity |
M | 0003746 | molecular_function | translation elongation factor activity |
M | 0005737 | cellular_component | cytoplasm |
M | 0006412 | biological_process | translation |
M | 0006414 | biological_process | translational elongation |
M | 0043043 | biological_process | peptide biosynthetic process |
N | 0003746 | molecular_function | translation elongation factor activity |
N | 0005737 | cellular_component | cytoplasm |
N | 0006412 | biological_process | translation |
N | 0006414 | biological_process | translational elongation |
N | 0043043 | biological_process | peptide biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue TYD A 401 |
Chain | Residue |
A | ASN13 |
A | TYR257 |
A | ARG270 |
A | GLY271 |
A | GLU272 |
A | ASP273 |
A | SER274 |
A | GOL402 |
A | TYR14 |
A | GLY15 |
A | ILE48 |
A | PHE190 |
A | TYR192 |
A | PHE251 |
A | MET252 |
A | GLN254 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | ASN13 |
A | TYR192 |
A | GLU272 |
A | TYR290 |
A | TYD401 |
M | ARG32 |
M | HOH212 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue TYD C 401 |
Chain | Residue |
C | ASN13 |
C | TYR14 |
C | GLY15 |
C | ILE48 |
C | PHE190 |
C | TYR192 |
C | PHE251 |
C | MET252 |
C | GLN254 |
C | TYR257 |
C | ARG270 |
C | GLY271 |
C | GLU272 |
C | ASP273 |
C | SER274 |
C | GOL402 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL C 402 |
Chain | Residue |
C | GLY15 |
C | GLU272 |
C | TYR290 |
C | TYD401 |
C | HOH603 |
N | ARG32 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | CARBOHYD: N-alpha-linked (Rha) arginine => ECO:0000269|PubMed:26060278, ECO:0000269|PubMed:28451135, ECO:0000269|PubMed:28451332, ECO:0000269|PubMed:31010899 |
Chain | Residue | Details |
M | ARG32 | |
N | ARG32 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:31010899 |
Chain | Residue | Details |
A | GLU272 | |
C | GLU272 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7K |
Chain | Residue | Details |
A | ASN13 | |
A | TYR192 | |
A | MET252 | |
A | ARG270 | |
C | ASN13 | |
C | TYR192 | |
C | MET252 | |
C | ARG270 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31010899, ECO:0007744|PDB:6J7L, ECO:0007744|PDB:6J7M |
Chain | Residue | Details |
A | TYR14 | |
C | TYR14 |