Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EJM

CRYSTAL STRUCTURE OF THE BPTI ALA16LEU MUTANT IN COMPLEX WITH BOVINE 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
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0004175	molecular_function	endopeptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
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	0046872	molecular_function	metal ion binding
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
E	0004175	molecular_function	endopeptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0006508	biological_process	proteolysis
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	0046872	molecular_function	metal ion binding
E	0097180	cellular_component	serine protease inhibitor complex
E	0097655	molecular_function	serpin family protein binding
F	0004867	molecular_function	serine-type endopeptidase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 3601

Chain	Residue
C	LYS60
C	HOH4359
D	ARG520
D	LYS546

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 3602

Chain	Residue
D	ARG542
F	ARG520
F	TYR535
F	HOH4284

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 3603

Chain	Residue
B	LYS541
B	ARG542
B	HOH4120
B	HOH4539
B	HOH4565
B	GLU507

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 3604

Chain	Residue
D	ARG520
D	TYR535
D	HOH4142
F	ARG542
F	HOH4399
F	HOH4538

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 3605

Chain	Residue
D	LYS541
D	SO43606
D	HOH4134
F	TYR510
F	ARG539
F	HOH4117

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 3606

Chain	Residue
D	TYR510
D	ARG539
F	TYR510
F	SO43605
F	HOH4298

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 3607

Chain	Residue
B	ARG520
B	TYR535
B	GLY537
B	ALA540
B	HOH4023
B	HOH4500

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 3608

Chain	Residue
E	ASN100
E	ASN101
E	ASN179
E	HOH4355

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 3609

Chain	Residue
A	LYS60
B	ILE519
B	ARG520
B	LYS546

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 3610

Chain	Residue
A	ASN100
A	ASN101
A	ASN179
A	HOH4203

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 3611

Chain	Residue
D	PRO509
D	TYR510
D	THR511
D	GLY512
D	HOH4469

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 3612

Chain	Residue
C	LYS169
C	PRO173
C	GLY174
C	HOH4048
C	HOH4510
C	HOH4576

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
A	VAL53-CYS58

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

Chain	Residue	Details
A	ASP189-VAL200

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

Chain	Residue	Details
B	PHE533-CYS551

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	660
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	9
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	21
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	150
Details	Domain: {"description":"BPTI/Kunitz inhibitor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
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	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57

site_id	CSA4
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	CSA5
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	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
A	ASP102
A	SER195
A	HIS57
A	GLY196

site_id	CSA8
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	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57
E	GLY196

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)