5NDD

Crystal structure of a thermostabilised human protease-activated receptor-2 (PAR2) in complex with AZ8838 at 2.8 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0005506	molecular_function	iron ion binding
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009055	molecular_function	electron transfer activity
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042597	cellular_component	periplasmic space
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue 8TZ A 2201

Chain	Residue
A	TYR82
A	HIS227
A	ASP228
A	ILE327
A	LEU330
A	LYS131
A	TYR134
A	HIS135
A	TRP141
A	ILE152
A	PHE155
A	TYR156
A	CYS226

---

site_id	AC2
Number of Residues	6
Details	binding site for residue NA A 2202

Chain	Residue
A	ASP121
A	ASN158
A	SER162
A	ASN336
A	ASP340
A	HOH2307

---

site_id	AC3
Number of Residues	5
Details	binding site for residue PO4 A 2203

Chain	Residue
A	GLN1141
A	THR1142
A	PRO1143
A	ASN1144
A	ARG1145

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	22
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	13
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	29
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	11
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	28
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	39
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	27
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	27
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	33
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	39
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"28445455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12171601","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASP1020	covalent catalysis

---