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 | 984 |
Details | TOPO_DOM: Periplasmic => ECO:0000305 |
Chain | Residue | Details |
A | ARG77-HIS323 | |
B | ARG77-HIS323 | |
C | ARG77-HIS323 | |
D | ARG77-HIS323 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | SER90 | |
A | LYS145 | |
B | SER90 | |
B | LYS145 | |
C | SER90 | |
C | LYS145 | |
D | SER90 | |
D | LYS145 |
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 |