2ERV
Crystal structure of the outer membrane enzyme PagL
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008653 | biological_process | lipopolysaccharide metabolic process |
A | 0009279 | cellular_component | cell outer membrane |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046493 | biological_process | lipid A metabolic process |
A | 0050528 | molecular_function | acyloxyacyl hydrolase activity |
B | 0008653 | biological_process | lipopolysaccharide metabolic process |
B | 0009279 | cellular_component | cell outer membrane |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046493 | biological_process | lipid A metabolic process |
B | 0050528 | molecular_function | acyloxyacyl hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 195 |
Chain | Residue |
A | ASP106 |
B | ASP106 |
B | CXE1200 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CXE B 196 |
Chain | Residue |
B | TRP25 |
B | TRP41 |
B | ILE83 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CXE B 200 |
Chain | Residue |
B | LEU132 |
A | ILE108 |
A | ALA124 |
B | ALA130 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CXE A 300 |
Chain | Residue |
A | TRP25 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CXE B 400 |
Chain | Residue |
B | MET15 |
B | VAL122 |
B | TYR142 |
B | SER143 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CXE B 500 |
Chain | Residue |
A | ILE75 |
B | GLY111 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CXE A 600 |
Chain | Residue |
A | MET15 |
A | TYR142 |
A | HOH859 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CXE A 700 |
Chain | Residue |
A | GLY111 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CXE A 800 |
Chain | Residue |
B | LEU19 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CXE B 900 |
Chain | Residue |
B | PHE62 |
B | PRO64 |
B | ILE83 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CXE B 1000 |
Chain | Residue |
B | VAL85 |
B | LEU102 |
B | PHE104 |
B | ASN129 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CXE B 1100 |
Chain | Residue |
A | ALA130 |
B | ILE83 |
B | ARG107 |
B | ILE108 |
B | GLU140 |
B | TYR142 |
B | CXE1200 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CXE B 1200 |
Chain | Residue |
A | PHE104 |
A | ASP106 |
A | SER128 |
A | CA195 |
B | PHE104 |
B | ASP106 |
B | HIS126 |
B | SER128 |
B | CXE1100 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 62 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:16632613 |
Chain | Residue | Details |
A | ASP2-ALA5 | |
B | ALA71-GLY72 | |
B | VAL93-GLY94 | |
B | HIS126-ILE150 | |
A | THR10 | |
A | GLU49-GLY50 | |
A | ALA71-GLY72 | |
A | VAL93-GLY94 | |
A | HIS126-ILE150 | |
B | ASP2-ALA5 | |
B | THR10 | |
B | GLU49-GLY50 |
site_id | SWS_FT_FI2 |
Number of Residues | 168 |
Details | TRANSMEM: Beta stranded => ECO:0000269|PubMed:16632613 |
Chain | Residue | Details |
A | ALA6-ALA9 | |
B | ALA6-ALA9 | |
B | GLY11-ASP26 | |
B | THR34-TRP48 | |
B | GLY51-PHE66 | |
B | TYR68-PHE70 | |
B | ASP73-ILE75 | |
B | PHE78-ARG92 | |
B | ASP95-GLU105 | |
B | ASN116-ILE125 | |
A | GLY11-ASP26 | |
A | THR34-TRP48 | |
A | GLY51-PHE66 | |
A | TYR68-PHE70 | |
A | ASP73-ILE75 | |
A | PHE78-ARG92 | |
A | ASP95-GLU105 | |
A | ASN116-ILE125 |
site_id | SWS_FT_FI3 |
Number of Residues | 34 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:16632613 |
Chain | Residue | Details |
A | LYS27-SER33 | |
A | VAL67 | |
A | LYS76-PRO77 | |
A | ASP106-ALA115 | |
B | LYS27-SER33 | |
B | VAL67 | |
B | LYS76-PRO77 | |
B | ASP106-ALA115 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:15611102 |
Chain | Residue | Details |
A | HIS126 | |
A | SER128 | |
B | HIS126 | |
B | SER128 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:16632613 |
Chain | Residue | Details |
A | GLU140 | |
B | GLU140 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Critical for activity => ECO:0000269|PubMed:16632613 |
Chain | Residue | Details |
A | ASN129 | |
B | ASN129 |