1BRC

RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005509	molecular_function	calcium ion binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0006508	biological_process	proteolysis
E	0007584	biological_process	response to nutrient
E	0007586	biological_process	digestion
E	0008233	molecular_function	peptidase activity
E	0008236	molecular_function	serine-type peptidase activity
E	0016787	molecular_function	hydrolase activity
E	0030574	biological_process	collagen catabolic process
E	0046872	molecular_function	metal ion binding
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity

Functional Information from PDB Data

site_id	CAT
Number of Residues	3
Details	CATALYTIC TRIAD RESIDUES, CONSERVED IN ALL SERINE PROTEASES OF THE TRYPSIN AND SUBTILISIN STRUCTURAL CLASSES

Chain	Residue
E	HIS57
E	ASP102
E	SER195

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Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC

Chain	Residue	Details
E	VAL53-CYS58

---

site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. GScqGDSGGPVV

Chain	Residue	Details
E	GLY189-VAL200

---

site_id	PS00280
Number of Residues	19
Details	BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FfyGGCggnrnnFdteeyC

Chain	Residue	Details
I	PHE33-CYS51

---

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	4
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Required for specificity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	50
Details	Domain: {"description":"BPTI/Kunitz inhibitor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Reactive bond"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}

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
E	ASP102
E	HIS57

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	SER195
E	GLY196

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	SER195
E	GLY193

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57
E	GLY196

---

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	GLY193
E	HIS57

---

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	SER195
E	GLY193
E	ASP95
E	HIS57

---