3URN

Crystal Structure of PTE mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with cyclohexyl methylphosphonate inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004063	molecular_function	aryldialkylphosphatase activity
A	0005886	cellular_component	plasma membrane
A	0008270	molecular_function	zinc ion binding
A	0009056	biological_process	catabolic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0046872	molecular_function	metal ion binding
B	0004063	molecular_function	aryldialkylphosphatase activity
B	0005886	cellular_component	plasma membrane
B	0008270	molecular_function	zinc ion binding
B	0009056	biological_process	catabolic process
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO A 801

Chain	Residue
A	KCX169
A	HIS201
A	HIS230
A	QMP902
A	HOH1361

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO A 802

Chain	Residue
A	HOH1361
A	HIS55
A	HIS57
A	KCX169
A	ASP301

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE QMP A 902

Chain	Residue
A	HIS57
A	GLY60
A	TRP131
A	PHE132
A	KCX169
A	HIS201
A	HIS230
A	ASP301
A	PHE306
A	CO801

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE IMD A 903

Chain	Residue
A	HIS230
A	ASP232
A	ASP233
A	ASP253
A	GLY254
A	TRP257
A	ARG280
A	ASP301

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO B 803

Chain	Residue
B	HIS55
B	HIS57
B	KCX169
B	ASP301
B	HOH1368

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO B 804

Chain	Residue
B	KCX169
B	HIS201
B	HIS230
B	QMP901
B	HOH1368

---

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE QMP B 901

Chain	Residue
B	HIS57
B	GLY60
B	TRP131
B	PHE132
B	KCX169
B	HIS201
B	TRP257
B	PHE306
B	CO804
B	IMD905
B	HOH1368

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IMD B 904

Chain	Residue
B	HIS230
B	ASP232
B	ASP233
B	ASP253
B	GLY254
B	TRP257
B	ASP301

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IMD B 905

Chain	Residue
B	SER308
B	QMP901

---

Functional Information from PROSITE/UniProt

site_id	PS01322
Number of Residues	9
Details	PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLtHEHI

Chain	Residue	Details
A	GLY50-ILE58

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
A	HIS55	metal ligand
A	HIS57	metal ligand
A	KCX169	metal ligand
A	SER205	metal ligand
A	THR234	metal ligand
A	LEU237	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	SER258	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	GLY305	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
B	HIS55	metal ligand
B	HIS57	metal ligand
B	KCX169	metal ligand
B	SER205	metal ligand
B	THR234	metal ligand
B	LEU237	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	SER258	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	GLY305	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

---