Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2D26

Active site distortion is sufficient for proteinase inhibit second crystal structure of covalent serpin-proteinase complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002020	molecular_function	protease binding
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005794	cellular_component	Golgi apparatus
A	0006953	biological_process	acute-phase response
A	0007596	biological_process	blood coagulation
A	0007599	biological_process	hemostasis
A	0030134	cellular_component	COPII-coated ER to Golgi transport vesicle
A	0030414	molecular_function	peptidase inhibitor activity
A	0031012	cellular_component	extracellular matrix
A	0031093	cellular_component	platelet alpha granule lumen
A	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
A	1904813	cellular_component	ficolin-1-rich granule lumen
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	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	MET53-CYS58

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

Chain	Residue	Details
C	SER185-HIS200

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. VKFNKPFVFlI

Chain	Residue	Details
B	VAL364-ILE374

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Site: {"description":"(Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur","evidences":[{"source":"PubMed","id":"3533918","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Site: {"description":"(Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases","evidences":[{"source":"PubMed","id":"3533918","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"S-cysteinyl cysteine"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16622833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16622833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16622833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"4578945","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"5415110","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"5415110","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7656008","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ELA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ELB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ELC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	HIS57

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	SER195
C	GLY196

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

Chain	Residue	Details
C	SER195
C	GLY193

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

Chain	Residue	Details
C	ASP102
C	SER195
C	HIS57

site_id	CSA5
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	CSA6
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	CSA7
Number of Residues	5
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	GLY193
C	HIS57
C	SER214

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