Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1A0J

CRYSTAL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED FISH SPECIES.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
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
B	0004252	molecular_function	serine-type endopeptidase activity
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
C	0004252	molecular_function	serine-type endopeptidase activity
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
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0006508	biological_process	proteolysis
D	0007586	biological_process	digestion
D	0008233	molecular_function	peptidase activity
D	0008236	molecular_function	serine-type peptidase activity
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 247

Chain	Residue
A	GLU70
A	ASN72
A	VAL75
A	GLU77
A	GLU80

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 248

Chain	Residue
A	SER195
A	HIS40
A	HIS57
A	GLN192
A	GLY193

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 249

Chain	Residue
A	PRO152
A	ASP153
A	THR154
A	ARG156

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 248

Chain	Residue
B	HIS57
B	GLN192
B	GLY193
B	SER195
B	BEN246
B	HOH323

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 249

Chain	Residue
B	PRO152
B	ASP153
B	THR154
B	ARG156

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 248

Chain	Residue
C	HIS57
C	GLN192
C	GLY193
C	SER195
C	BEN246
C	HOH614

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 249

Chain	Residue
C	GLU21
C	PRO152
C	ASP153
C	THR154
C	ARG156

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 248

Chain	Residue
A	TYR39
D	HIS57
D	GLN192
D	GLY193
D	SER195
D	BEN246

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 249

Chain	Residue
A	ASN76
B	ARG235
D	PRO152
D	ASP153
D	THR154
D	ARG156

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 250

Chain	Residue
A	SER148
A	SER149
C	ASN95
C	ARG97
D	ARG62
D	HOH490

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 251

Chain	Residue
C	SER96
D	LYS60
D	SER61
D	HOH474
D	HOH503

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BEN A 246

Chain	Residue
A	ASP189
A	SER190
A	SER195
A	GLY219
A	CYS220
A	GLY226

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BEN B 246

Chain	Residue
B	ASP189
B	SER190
B	SER195
B	GLY219
B	GLY226
B	SO4248

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BEN C 246

Chain	Residue
C	ASP189
C	SER190
C	CYS191
C	SER195
C	GLY219
C	GLY226
C	SO4248
C	HOH312

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BEN D 246

Chain	Residue
D	ASP189
D	SER190
D	CYS191
D	SER195
D	GLY219
D	GLY226
D	SO4248

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Charge relay system => ECO:0000250

Chain	Residue	Details
A	HIS57
D	HIS57
D	ASP102
D	SER195
A	ASP102
A	SER195
B	HIS57
B	ASP102
B	SER195
C	HIS57
C	ASP102
C	SER195

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLU70
D	GLU70
D	ASN72
D	GLU80
A	ASN72
A	GLU80
B	GLU70
B	ASN72
B	GLU80
C	GLU70
C	ASN72
C	GLU80

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	VAL75
B	VAL75
C	VAL75
D	VAL75

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Required for specificity => ECO:0000250

Chain	Residue	Details
A	ASP189
B	ASP189
C	ASP189
D	ASP189

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