1T7C

CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

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	7
Details	BINDING SITE FOR RESIDUE SO4 B 601

Chain	Residue
B	PHE4
B	GLU7
B	ARG42
B	HOH2010
B	HOH2061
B	HOH2286
D	TYR10

---

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

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

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 603

Chain	Residue
B	TYR10
B	HOH2016
B	HOH2138
B	HOH2265
D	PHE4
D	ARG42

---

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

Chain	Residue
B	PRO2
B	ASP3
B	HOH2011
B	HOH2173
B	HOH2194
B	HOH2430
C	TYR171
C	TRP172
C	SER217
C	SER218
C	HOH2106

---

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	HOH2007
A	HOH2033
A	HOH2074
A	HOH2184
A	HOH2329
D	PRO2
D	ASP3

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 606

Chain	Residue
A	LYS90
A	ASN91
A	SER92
A	TRP237
A	HOH2396
A	HOH2476

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 607

Chain	Residue
A	ASN100
A	ASN101
A	HOH2132

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 1602

Chain	Residue
A	LEU97
C	HOH1660
D	ARG20
D	TYR35
D	GLY37
D	ALA40
D	HOH2455

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 1606

Chain	Residue
C	LYS90
C	ASN91
C	SER92
C	TRP237
C	HOH2201
C	HOH2202
C	HOH2346

---

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

---