1P2Q

Structural consequences of accommodation of four non-cognate amino-acid residues in the S1 pocket of bovine trypsin and chymotrypsin

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	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	0097180	cellular_component	serine protease inhibitor complex
A	0097655	molecular_function	serpin family protein binding
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0007586	biological_process	digestion
C	0008233	molecular_function	peptidase activity
C	0008236	molecular_function	serine-type peptidase activity
C	0016787	molecular_function	hydrolase activity
C	0097180	cellular_component	serine protease inhibitor complex
C	0097655	molecular_function	serpin family protein binding
D	0004867	molecular_function	serine-type endopeptidase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 601

Chain	Residue
B	PHE4
B	GLU7
B	ARG42
B	HOH2012
B	HOH2320
D	TYR10
D	LYS41
D	HOH2153

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 602

Chain	Residue
B	ARG20
B	TYR35
B	GLY37
B	HOH682
C	LEU97
A	HOH660

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 603

Chain	Residue
B	TYR10
B	LYS41
B	HOH2107
B	HOH2339
D	PHE4
D	GLU7
D	ARG42
D	HOH2019

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 B 604

Chain	Residue
B	PRO2
B	ASP3
B	HOH2078
B	HOH2307
B	HOH2500
C	TYR171
C	TRP172
C	SER217
C	SER218
C	HOH2028
C	HOH2157

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 A 605

Chain	Residue
A	TYR171
A	TRP172
A	SER217
A	SER218
A	HOH2022
A	HOH2060
A	HOH2409
D	PRO2
D	ASP3
D	HOH2084
D	HOH2171

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 1602

Chain	Residue
A	LEU97
C	HOH1660
D	ARG20
D	TYR35
D	GLY37

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1607

Chain	Residue
A	ASN95
A	ASN100
A	ASN101
A	HOH2141
A	HOH2335

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1608

Chain	Residue
A	LYS90
A	ASN91
A	SER92
A	TRP237
A	HOH2418
A	HOH2442

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 1609

Chain	Residue
C	LYS90
C	SER92
C	TRP237
C	HOH2123
C	HOH2175
C	HOH2399

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 1610

Chain	Residue
C	ASN95
C	ASN100
C	ASN101
C	HOH2156
C	HOH2406

---

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS A 3000

Chain	Residue
A	ASP35
A	PHE41
A	CYS58
A	GLY59
A	ASP64
A	HOH2381
B	ILE18
B	HOH2257

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS C 3001

Chain	Residue
C	ASP35
C	PHE41
C	CYS58
C	GLY59
C	THR61
C	ASP64
C	HOH2226

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL53-CYS58

---

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

Chain	Residue	Details
A	SER189-VAL200

---

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

Chain	Residue	Details
B	PHE33-CYS51

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	100
Details	Domain: {"description":"BPTI/Kunitz inhibitor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Reactive bond for trypsin"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	HIS57

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	HIS57

---

site_id	CSA3
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	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	GLY193
C	HIS57

---

site_id	CSA5
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	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	HIS57
C	GLY196

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 387

Chain	Residue	Details
A	HIS57	electrostatic stabiliser, proton shuttle (general acid/base)
A	ASP102	modifies pKa
A	GLY193	electrostatic stabiliser
A	SER195	covalent catalysis
A	GLY196	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 387

Chain	Residue	Details
C	HIS57	electrostatic stabiliser, proton shuttle (general acid/base)
C	ASP102	modifies pKa
C	GLY193	electrostatic stabiliser
C	SER195	covalent catalysis
C	GLY196	electrostatic stabiliser

---