Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3E8L

The Crystal Structure of the Double-headed Arrowhead Protease Inhibitor A in Complex with Two Trypsins

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	0004175	molecular_function	endopeptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006508	biological_process	proteolysis
B	0007586	biological_process	digestion
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0097180	cellular_component	serine protease inhibitor complex
B	0097655	molecular_function	serpin family protein binding
C	0004866	molecular_function	endopeptidase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 178

Chain	Residue
C	GLN12
C	LEU21
C	TYR22
C	LYS175
C	PHE176

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 179

Chain	Residue
C	TYR134
C	PRO2
C	VAL4
C	LEU73
C	THR131

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 180

Chain	Residue
A	TYR37
C	HOH218

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT C 181

Chain	Residue
A	GOL2
A	VAL73
C	SER64
C	ALA65

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 182

Chain	Residue
A	SER110
C	LEU13
C	LEU15
C	GLY16
C	ASN18
C	PRO20

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 183

Chain	Residue
B	GLY143
C	LYS78
C	TRP122

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 1

Chain	Residue
A	THR122
A	SER123
A	LYS201

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 3

Chain	Residue
A	GLN170
A	SER210
A	HOH250
A	HOH289

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 5

Chain	Residue
A	HIS38
A	CYS40
A	GLY190
A	HOH253

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA A 7

Chain	Residue
A	ACT6
A	HIS38

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 8

Chain	Residue
A	GLY60
A	LYS215

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA A 10

Chain	Residue
A	LYS232

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 2

Chain	Residue
A	ASN94
A	THR95
A	LEU96
A	GLN170
A	TRP208
A	HOH268
A	HOH299
C	PHE143
C	ACT181

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 239

Chain	Residue
A	SER35
A	TYR37
A	PHE39
A	LYS58
A	HOH297
C	PRO149

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 12

Chain	Residue
A	GLN130
A	CYS131
A	VAL197
A	CYS198
A	SER199
A	GLY200

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 240

Chain	Residue
A	SER81
A	LYS106
A	GLN214
A	LYS215

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 6

Chain	Residue
A	NA7
A	TYR37
A	HIS38
A	HOH315
C	ARG126

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA B 6

Chain	Residue
B	LYS140
B	SER142

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA B 11

Chain	Residue
B	GLY60

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1

Chain	Residue
B	ASN94
B	THR95
B	GLN170
B	TRP208
C	PRO84

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 3

Chain	Residue
B	GLN189
B	GLY211
B	CYS212
B	HOH271
C	THR91

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 239

Chain	Residue
B	SER85
B	ILE86
B	VAL87

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 7

Chain	Residue
B	EDO8
B	CYS124
B	ALA125
B	ASP160
B	GLN203
B	LYS223
B	CYS225
B	HOH279

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 8

Chain	Residue
B	MET175
B	LYS223
B	EDO7
B	ASP160
B	THR172
B	SER173

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 240

Chain	Residue
B	ASN97
B	ASN98
B	SER173
B	ASN174

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT B 2

Chain	Residue
B	HIS55
C	TYR114

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	VAL51-CYS56

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

Chain	Residue	Details
A	ASP186-VAL197

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	440
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	6
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {}

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	SER192
A	ASP99
A	HIS55

site_id	CSA10
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	SER192
B	ASP99
B	HIS55
B	GLY190

site_id	CSA11
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER192
A	GLY193
A	ASP99
A	HIS55

site_id	CSA12
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	SER192
B	GLY193
B	ASP99
B	HIS55

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

Chain	Residue	Details
B	SER192
B	ASP99
B	HIS55

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

Chain	Residue	Details
A	ASP99
A	HIS55

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP99
B	HIS55

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER192
A	GLY190

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	SER192
B	GLY190

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER192
A	GLY193

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	SER192
B	GLY193

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

Chain	Residue	Details
A	SER192
A	ASP99
A	HIS55
A	GLY190

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