Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ZA5

Crystal Structure of human tryptase with potent non-peptide inhibitor

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	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0031012	cellular_component	extracellular matrix
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	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0016787	molecular_function	hydrolase activity
B	0031012	cellular_component	extracellular matrix
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	0008233	molecular_function	peptidase activity
C	0008236	molecular_function	serine-type peptidase activity
C	0016787	molecular_function	hydrolase activity
C	0031012	cellular_component	extracellular matrix
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008236	molecular_function	serine-type peptidase activity
D	0016787	molecular_function	hydrolase activity
D	0031012	cellular_component	extracellular matrix

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 2FF B 1

Chain	Residue
B	GLN102
B	GLY230
B	GLU231
B	GLY232
B	HOH305
D	ASP64
D	TYR99
B	TYR177
B	ILE189
B	ASP203
B	SER204
B	CYS205
B	GLN206
B	SER209
B	TRP229

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 2FF A 4

Chain	Residue
A	TYR177
A	ASP203
A	SER204
A	CYS205
A	GLN206
A	SER209
A	TRP229
A	GLY230
A	GLU231
A	GLY232
A	ARG238
A	GLY240
A	HOH272
C	ASP64

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 2FF D 3

Chain	Residue
B	ASP64
D	TYR177
D	ILE189
D	ASP203
D	SER204
D	CYS205
D	GLN206
D	SER209
D	TRP229
D	GLY230
D	GLU231
D	GLY232
D	ARG238

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 2FF C 2

Chain	Residue
A	ASP64
C	GLN102
C	TYR177
C	ILE189
C	ASP203
C	SER204
C	CYS205
C	GLN206
C	SER209
C	TRP229
C	GLY230
C	GLU231
C	GLY232
C	ARG238
C	HOH263
C	HOH285

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU55-CYS60

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

Chain	Residue	Details
A	ASP203-VAL214

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	964
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	12
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P21845","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

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	SER209
A	ASP106
A	HIS59

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP106
A	HIS59

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP106
B	HIS59

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP106
C	HIS59

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	ASP106
D	HIS59

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	GLY207
A	SER209

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	GLY207
B	SER209

site_id	CSA16
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	GLY207
D	SER209

site_id	CSA17
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER209
A	GLY210

site_id	CSA18
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	SER209
B	GLY210

site_id	CSA19
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	SER209
C	GLY210

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

Chain	Residue	Details
B	SER209
B	ASP106
B	HIS59

site_id	CSA20
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	SER209
D	GLY210

site_id	CSA21
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	GLY207
A	SER209
A	ASP106
A	HIS59

site_id	CSA22
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	GLY207
B	SER209
B	ASP106
B	HIS59

site_id	CSA23
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	GLY207
C	SER209
C	ASP106
C	HIS59

site_id	CSA24
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	GLY207
D	SER209
D	ASP106
D	HIS59

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	SER209
C	ASP106
C	HIS59

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	SER209
D	ASP106
D	HIS59

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

Chain	Residue	Details
A	SER209
A	ASP106
A	HIS59
A	GLY210

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

Chain	Residue	Details
B	SER209
B	ASP106
B	HIS59
B	GLY210

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	SER209
C	ASP106
C	HIS59
C	GLY210

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

Chain	Residue	Details
D	SER209
D	ASP106
D	HIS59
D	GLY210

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	GLY207
C	SER209

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)