8EXR
Cryo-EM structure of S. aureus BlaR1 TM and zinc metalloprotease domain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0008658 | molecular_function | penicillin binding |
A | 0071555 | biological_process | cell wall organization |
B | 0005886 | cellular_component | plasma membrane |
B | 0008658 | molecular_function | penicillin binding |
B | 0071555 | biological_process | cell wall organization |
C | 0005886 | cellular_component | plasma membrane |
C | 0008658 | molecular_function | penicillin binding |
C | 0071555 | biological_process | cell wall organization |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 942 |
Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P12287 |
Chain | Residue | Details |
B | MET1-LEU4 | |
B | PRO49-ASN104 | |
B | LEU329-GLN585 | |
A | MET1-LEU4 | |
A | PRO49-ASN104 | |
A | LEU329-GLN585 | |
C | MET1-LEU4 | |
C | PRO49-ASN104 | |
C | LEU329-GLN585 |
site_id | SWS_FT_FI2 |
Number of Residues | 198 |
Details | TRANSMEM: Helical => ECO:0000250|UniProtKB:P12287 |
Chain | Residue | Details |
B | LEU5-PHE22 | |
C | TYR32-ILE48 | |
C | ILE105-LEU122 | |
C | ILE312-PHE328 | |
B | TYR32-ILE48 | |
B | ILE105-LEU122 | |
B | ILE312-PHE328 | |
A | LEU5-PHE22 | |
A | TYR32-ILE48 | |
A | ILE105-LEU122 | |
A | ILE312-PHE328 | |
C | LEU5-PHE22 |
site_id | SWS_FT_FI3 |
Number of Residues | 588 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P12287 |
Chain | Residue | Details |
B | ARG23-ASN31 | |
B | LYS123-LEU311 | |
A | ARG23-ASN31 | |
A | LYS123-LEU311 | |
C | ARG23-ASN31 | |
C | LYS123-LEU311 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | ACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:15506754, ECO:0000269|PubMed:21775440 |
Chain | Residue | Details |
B | SER389 | |
A | SER389 | |
C | SER389 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12591921 |
Chain | Residue | Details |
B | LYS392 | |
A | LYS392 | |
C | LYS392 |