6TH7
Structure of porcine pancreatic elastase in complex with tutuilamide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 301 |
Chain | Residue |
A | GLU85 |
A | ASN87 |
A | GLN90 |
A | ASP92 |
A | GLU95 |
A | HOH501 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CA B 301 |
Chain | Residue |
B | ASP92 |
B | GLU95 |
B | GLU85 |
B | ASN87 |
B | GLN90 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for Di-peptide ABA A 301 and ILE A 306 |
Chain | Residue |
A | HIS71 |
A | VAL114 |
A | SER233 |
A | PHE234 |
A | VAL235 |
A | SER236 |
A | ARG237 |
C | VAL302 |
C | 5XU309 |
C | N9K303 |
C | AA4305 |
C | ABA306 |
C | HOH401 |
C | HOH403 |
C | HOH405 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residues ABA A 301 and ABA A 310 |
Chain | Residue |
A | HIS71 |
A | VAL114 |
A | GLN211 |
A | GLY212 |
A | SER214 |
A | SER233 |
A | PHE234 |
A | VAL235 |
C | VAL302 |
C | ILE308 |
C | AA4305 |
C | HOH401 |
C | HOH403 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for Di-peptide ABA A 301 and VAL A 302 |
Chain | Residue |
A | HIS71 |
A | VAL114 |
A | SER233 |
C | ILE308 |
C | N9K303 |
C | AA4305 |
C | ABA306 |
C | HOH401 |
C | HOH403 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for Di-peptide VAL A 302 and N9K A 307 |
Chain | Residue |
A | HIS71 |
A | PRO107 |
A | TRP258 |
C | ABA307 |
C | ILE308 |
C | PHE304 |
C | AA4305 |
C | HOH402 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residues O4Q A 304 and 5XU A 305 |
Chain | Residue |
A | PHE234 |
A | VAL235 |
A | SER236 |
A | ARG237 |
C | ILE308 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for Di-peptide 5XU A 305 and ILE A 306 |
Chain | Residue |
A | PHE234 |
A | VAL235 |
A | SER236 |
A | ARG237 |
C | ABA307 |
C | O4Q310 |
C | N9K303 |
C | ABA306 |
C | HOH405 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residues N9K A 307 and PHA A 308 |
Chain | Residue |
A | PRO107 |
A | GLN211 |
A | GLY212 |
A | TRP258 |
C | VAL302 |
C | ILE308 |
C | AA4305 |
C | HOH402 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residues PHA A 308 and AA4 A 309 |
Chain | Residue |
A | THR55 |
A | HIS71 |
A | PRO107 |
A | GLN211 |
A | GLY212 |
A | SER214 |
C | ABA307 |
C | VAL302 |
C | N9K303 |
C | ABA306 |
C | HOH401 |
C | HOH404 |
site_id | AD2 |
Number of Residues | 12 |
Details | binding site for residues PHA A 308 and AA4 A 309 |
Chain | Residue |
C | ABA306 |
C | HOH401 |
C | HOH404 |
A | THR55 |
A | HIS71 |
A | PRO107 |
A | GLN211 |
A | GLY212 |
A | SER214 |
C | ABA307 |
C | VAL302 |
C | N9K303 |
site_id | AD3 |
Number of Residues | 15 |
Details | binding site for residues AA4 A 309 and ABA A 310 |
Chain | Residue |
A | THR55 |
A | HIS71 |
A | GLN211 |
A | GLY212 |
A | SER214 |
A | SER233 |
A | PHE234 |
A | VAL235 |
C | ABA307 |
C | VAL302 |
C | ILE308 |
C | N9K303 |
C | PHE304 |
C | HOH401 |
C | HOH404 |
site_id | AD4 |
Number of Residues | 12 |
Details | binding site for residues ABA B 301 and ABA B 310 |
Chain | Residue |
B | HIS71 |
B | VAL114 |
B | GLN211 |
B | GLY212 |
B | SER214 |
B | SER233 |
B | VAL235 |
D | VAL314 |
D | ILE316 |
D | AA4311 |
B | HOH420 |
D | HOH401 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for Di-peptide ABA B 301 and VAL B 302 |
Chain | Residue |
B | HIS71 |
B | VAL114 |
B | SER233 |
D | ILE316 |
D | YNM313 |
D | AA4311 |
D | ABA310 |
D | HOH401 |
site_id | AD6 |
Number of Residues | 13 |
Details | binding site for Di-peptide ABA B 301 and ILE B 306 |
Chain | Residue |
A | ALA126 |
A | GLN127 |
B | HIS71 |
B | VAL114 |
B | SER233 |
B | PHE234 |
B | VAL235 |
D | VAL314 |
D | 5XU317 |
D | YNM313 |
D | AA4311 |
D | ABA310 |
D | HOH401 |
site_id | AD7 |
Number of Residues | 10 |
Details | binding site for Di-peptide VAL B 302 and YNM B 307 |
Chain | Residue |
A | PHE79 |
A | GLY99 |
A | VAL100 |
B | HIS71 |
D | ABA315 |
D | ILE316 |
D | PHE312 |
D | AA4311 |
D | ABA310 |
D | HOH402 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residues O4Q B 304 and 5XU B 305 |
Chain | Residue |
B | TRP190 |
B | PHE234 |
B | VAL235 |
B | SER236 |
B | ARG237 |
D | ILE316 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for Di-peptide 5XU B 305 and ILE B 306 |
Chain | Residue |
A | ALA126 |
A | GLN127 |
B | PHE234 |
B | VAL235 |
D | ABA315 |
D | O4Q318 |
D | YNM313 |
D | ABA310 |
site_id | AE1 |
Number of Residues | 10 |
Details | binding site for residues YNM B 307 and PHA B 308 |
Chain | Residue |
A | ARG47 |
A | PHE79 |
A | GLY99 |
A | VAL100 |
B | THR55 |
B | GLY212 |
D | VAL314 |
D | ILE316 |
D | AA4311 |
D | HOH402 |
site_id | AE2 |
Number of Residues | 11 |
Details | binding site for residues PHA B 308 and AA4 B 309 |
Chain | Residue |
A | ARG47 |
B | THR55 |
B | HIS71 |
B | GLN211 |
B | GLY212 |
B | SER214 |
D | ABA315 |
D | VAL314 |
D | YNM313 |
D | ABA310 |
D | HOH401 |
site_id | AE3 |
Number of Residues | 11 |
Details | binding site for residues PHA B 308 and AA4 B 309 |
Chain | Residue |
A | ARG47 |
B | THR55 |
B | HIS71 |
B | GLN211 |
B | GLY212 |
B | SER214 |
D | ABA315 |
D | VAL314 |
D | YNM313 |
D | ABA310 |
D | HOH401 |
site_id | AE4 |
Number of Residues | 14 |
Details | binding site for residues AA4 B 309 and ABA B 310 |
Chain | Residue |
B | THR55 |
B | HIS71 |
B | GLN211 |
B | GLY212 |
B | SER214 |
B | SER233 |
B | VAL235 |
D | ABA315 |
D | VAL314 |
D | ILE316 |
D | YNM313 |
D | PHE312 |
B | HOH420 |
D | HOH401 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 474 |
Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"4578945","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"5415110","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"5415110","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"7656008","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ELA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ELB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ELC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |