1NTP
USE OF THE NEUTRON DIFFRACTION H/D EXCHANGE TECHNIQUE TO DETERMINE THE CONFORMATIONAL DYNAMICS OF TRYPSIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004175 | molecular_function | endopeptidase activity |
| 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 | 0007586 | biological_process | digestion |
| 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 |
| A | 0097180 | cellular_component | serine protease inhibitor complex |
| A | 0097655 | molecular_function | serpin family protein binding |
Functional Information from PDB Data
| site_id | BIN |
| Number of Residues | 10 |
| Details | SPECIFIC BINDING POCKET: ASP-189 AT THE BOTTOM OF THIS POCKET FORMS AN H-BOND TO THE POSITIVELY CHARGED SIDE CHAIN OF A SPECIFIC SUBSTRATE, GIVING TRYPSIN ITS SPECIFICITY FOR THIS TYPE OF SIDE CHAIN. THE BACKBONE IN THE REGION FROM SER-214 TO CYS-220 IS INVOLVED IN HYDROGEN BONDING TO A PEPTIDE SUBSTRATE |
| Chain | Residue |
| A | TRP215 |
| A | GLY216 |
| A | SER217 |
| A | GLY219 |
| A | CYS220 |
| A | ASP189 |
| A | SER190 |
| A | CYS191 |
| A | GLN192 |
| A | SER214 |
| site_id | CAT |
| Number of Residues | 4 |
| Details | CATALYTIC SITE: THE OG ATOM OF SER-195 NUCLEOPHILICALLY ATTACKS THE SUBSTRATE CARBONYL CARBON ATOM. ASP-102 AND HIS-57 TOGETHER PROVIDE GENERAL BASE CATALYSIS. THE N-H GROUPS OF GLY-193 AND SER-195 STABILIZE REACTION INTERMEDIATES THROUGH H-BONDS TO THE SUBSTRATE CARBONYL OXYGEN ATOM. |
| Chain | Residue |
| A | HIS57 |
| A | ASP102 |
| A | GLY193 |
| A | SER195 |
| site_id | ION |
| Number of Residues | 11 |
| Details | CONTAINS A TIGHTLY BOUND POSITIVE ION WHICH IS PROBABLY A CA2+ IN THIS STRUCTURE. THE ION IS COORDINATED IN A ROUGHLY OCTAHEDRAL FASHION BY GLU 70, ASN 72, VAL 75, GLU 80, HOH 53 AND HOH 54. THIS REGION WAS FIRST IDENTIFIED AS THE PRIMARY CA2+ BINDING SITE OF TRYPSIN BY BODE AND SCHWAGER, F.E.B.S. LETT., VOL. 56, P139 (1975) |
| Chain | Residue |
| A | GLU70 |
| A | ASP71 |
| A | ASN72 |
| A | ILE73 |
| A | ASN74 |
| A | VAL75 |
| A | VAL76 |
| A | GLU77 |
| A | GLY78 |
| A | ASN79 |
| A | GLU80 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 220 |
| 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 | 3 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY196 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY193 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | HIS57 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | GLY193 | |
| A | HIS57 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 | |
| A | GLY196 |
| site_id | CSA7 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | GLY193 | |
| A | HIS57 | |
| A | SER214 |
