1B12
CRYSTAL STRUCTURE OF TYPE 1 SIGNAL PEPTIDASE FROM ESCHERICHIA COLI IN COMPLEX WITH A BETA-LACTAM INHIBITOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006465 | biological_process | signal peptide processing |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016020 | cellular_component | membrane |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006465 | biological_process | signal peptide processing |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0016020 | cellular_component | membrane |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006465 | biological_process | signal peptide processing |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0016020 | cellular_component | membrane |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006465 | biological_process | signal peptide processing |
| D | 0006508 | biological_process | proteolysis |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1002 |
| Chain | Residue |
| B | GLU163 |
| B | ARG226 |
| B | HOH1053 |
| B | HOH1055 |
| B | HOH1066 |
| C | SER161 |
| C | GLU163 |
| C | ARG226 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PN B 1001 |
| Chain | Residue |
| B | PRO87 |
| B | SER88 |
| B | SER90 |
| B | TYR143 |
| B | ILE144 |
| B | LYS145 |
| B | SER278 |
| B | ALA279 |
| B | ILE86 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 1PN C 1001 |
| Chain | Residue |
| C | ILE86 |
| C | PRO87 |
| C | SER88 |
| C | SER90 |
| C | ASP142 |
| C | TYR143 |
| C | ILE144 |
| C | LYS145 |
| C | SER278 |
| C | ALA279 |
| C | HOH1048 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PN A 1001 |
| Chain | Residue |
| A | ILE86 |
| A | PRO87 |
| A | SER88 |
| A | SER90 |
| A | TYR143 |
| A | ILE144 |
| A | LYS145 |
| A | SER278 |
| A | ALA279 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PN D 1001 |
| Chain | Residue |
| D | ILE86 |
| D | PRO87 |
| D | SER88 |
| D | SER90 |
| D | ILE144 |
| D | LYS145 |
| D | SER278 |
| D | ALA279 |
Functional Information from PROSITE/UniProt
| site_id | PS00501 |
| Number of Residues | 8 |
| Details | SPASE_I_1 Signal peptidases I serine active site. SGSMMPTL |
| Chain | Residue | Details |
| A | SER88-LEU95 |
| site_id | PS00760 |
| Number of Residues | 13 |
| Details | SPASE_I_2 Signal peptidases I lysine active site. KRAVGlPGDkVtY |
| Chain | Residue | Details |
| A | LYS145-TYR157 |
| site_id | PS00761 |
| Number of Residues | 14 |
| Details | SPASE_I_3 Signal peptidases I signature 3. YFMMGDNRdnSadS |
| Chain | Residue | Details |
| A | TYR268-SER281 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1t7d |
| Chain | Residue | Details |
| A | SER90 | |
| A | LYS145 | |
| A | SER88 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1t7d |
| Chain | Residue | Details |
| B | SER90 | |
| B | LYS145 | |
| B | SER88 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1t7d |
| Chain | Residue | Details |
| C | SER90 | |
| C | LYS145 | |
| C | SER88 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1t7d |
| Chain | Residue | Details |
| D | SER90 | |
| D | LYS145 | |
| D | SER88 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 635 |
| Chain | Residue | Details |
| A | SER88 | electrostatic stabiliser |
| A | SER90 | nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LYS145 | proton acceptor, proton donor |
| A | SER278 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 635 |
| Chain | Residue | Details |
| B | SER88 | electrostatic stabiliser |
| B | SER90 | nucleofuge, nucleophile, proton acceptor, proton donor |
| B | LYS145 | proton acceptor, proton donor |
| B | SER278 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 635 |
| Chain | Residue | Details |
| C | SER88 | electrostatic stabiliser |
| C | SER90 | nucleofuge, nucleophile, proton acceptor, proton donor |
| C | LYS145 | proton acceptor, proton donor |
| C | SER278 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 635 |
| Chain | Residue | Details |
| D | SER88 | electrostatic stabiliser |
| D | SER90 | nucleofuge, nucleophile, proton acceptor, proton donor |
| D | LYS145 | proton acceptor, proton donor |
| D | SER278 | electrostatic stabiliser |
