Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0008360 | biological_process | regulation of cell shape |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0015648 | molecular_function | lipid-linked peptidoglycan transporter activity |
A | 0015836 | biological_process | lipid-linked peptidoglycan transport |
A | 0034204 | biological_process | lipid translocation |
A | 0071555 | biological_process | cell wall organization |
B | 0005886 | cellular_component | plasma membrane |
B | 0008360 | biological_process | regulation of cell shape |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0015648 | molecular_function | lipid-linked peptidoglycan transporter activity |
B | 0015836 | biological_process | lipid-linked peptidoglycan transport |
B | 0034204 | biological_process | lipid translocation |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue NA A 501 |
Chain | Residue |
A | ASP235 |
A | ASN374 |
A | ASP378 |
A | VAL390 |
A | ALA393 |
A | THR394 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CL A 502 |
Chain | Residue |
A | TYR41 |
A | ILE45 |
A | ARG255 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CL A 503 |
Chain | Residue |
A | LYS71 |
A | HIS210 |
A | HIS213 |
A | CL504 |
A | ZN505 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CL A 504 |
Chain | Residue |
A | HIS210 |
A | HIS213 |
A | CL503 |
A | ZN505 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN A 505 |
Chain | Residue |
A | HIS210 |
A | HIS213 |
A | CL503 |
A | CL504 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue OLB A 506 |
Chain | Residue |
A | TYR175 |
A | ILE178 |
A | SER179 |
A | ILE182 |
A | GLY183 |
B | GLU70 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL B 501 |
Chain | Residue |
B | TYR41 |
B | ARG255 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue CL B 502 |
Chain | Residue |
B | LYS71 |
B | HIS210 |
B | HIS213 |
B | CL503 |
B | ZN504 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL B 503 |
Chain | Residue |
B | LYS71 |
B | HIS210 |
B | CL502 |
B | ZN504 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN B 504 |
Chain | Residue |
B | HIS210 |
B | HIS213 |
B | CL502 |
B | CL503 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | MET1-SER2 | |
B | GLU57-LYS78 | |
B | LEU145-LYS150 | |
B | LYS197-HIS213 | |
B | VAL272-LEU287 | |
B | TYR354-THR362 | |
B | SER408-ASP416 | |
B | TYR462-LYS475 | |
A | GLU57-LYS78 | |
A | LEU145-LYS150 | |
A | LYS197-HIS213 | |
A | VAL272-LEU287 | |
A | TYR354-THR362 | |
A | SER408-ASP416 | |
A | TYR462-LYS475 | |
B | MET1-SER2 | |
Chain | Residue | Details |
A | ILE3-PHE23 | |
A | ILE333-SER353 | |
A | PRO363-LEU383 | |
A | PRO387-PHE407 | |
A | PHE417-THR437 | |
A | PHE441-PHE461 | |
B | ILE3-PHE23 | |
B | TYR36-GLY56 | |
B | PHE79-TYR99 | |
B | LEU124-ILE144 | |
B | PHE151-LEU171 | |
A | TYR36-GLY56 | |
B | GLY176-ILE196 | |
B | PHE214-VAL238 | |
B | LEU250-VAL271 | |
B | ASN288-LEU308 | |
B | ILE333-SER353 | |
B | PRO363-LEU383 | |
B | PRO387-PHE407 | |
B | PHE417-THR437 | |
B | PHE441-PHE461 | |
A | PHE79-TYR99 | |
A | LEU124-ILE144 | |
A | PHE151-LEU171 | |
A | GLY176-ILE196 | |
A | PHE214-VAL238 | |
A | LEU250-VAL271 | |
A | ASN288-LEU308 | |
Chain | Residue | Details |
A | ARG24-SER35 | |
B | SER172-TYR175 | |
B | VAL239-TYR249 | |
B | SER309-LYS332 | |
B | LYS384-GLY386 | |
B | ASP438-GLU440 | |
A | PHE100-LYS123 | |
A | SER172-TYR175 | |
A | VAL239-TYR249 | |
A | SER309-LYS332 | |
A | LYS384-GLY386 | |
A | ASP438-GLU440 | |
B | ARG24-SER35 | |
B | PHE100-LYS123 | |