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
| site_id | SWS_FT_FI1 |
| Number of Residues | 148 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 530 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 146 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]} |
