6FRZ

Phosphotriesterase PTE_A53_7

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	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	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	8
Details	binding site for residue FMT A 401

Chain	Residue
A	HIS55
A	HIS57
A	LYS169
A	HIS201
A	HIS230
A	ZN402
A	ZN403
A	E4T404

---

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 402

Chain	Residue
A	HIS57
A	ASP301
A	FMT401
A	E4T404
A	HIS55

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 403

Chain	Residue
A	HIS201
A	HIS230
A	FMT401
A	E4T404

---

site_id	AC4
Number of Residues	12
Details	binding site for residue E4T A 404

Chain	Residue
A	HIS55
A	HIS57
A	TRP131
A	HIS201
A	HIS230
A	ASP301
A	PHE306
A	FMT401
A	ZN402
A	ZN403
A	TRS405
A	HOH518

---

site_id	AC5
Number of Residues	8
Details	binding site for residue TRS A 405

Chain	Residue
A	HIS201
A	HIS230
A	ASP233
A	HIS257
A	LEU271
A	ARG280
A	E4T404
A	HOH565

---

site_id	AC6
Number of Residues	4
Details	binding site for residue P6G A 406

Chain	Residue
A	ARG41
A	PRO43
A	ARG118
A	HOH600

---

site_id	AC7
Number of Residues	4
Details	binding site for residue PEG A 407

Chain	Residue
A	ARG337
A	GLN343
A	THR350
A	VAL351

---

site_id	AC8
Number of Residues	9
Details	binding site for residue PGE A 408

Chain	Residue
A	LEU130
A	TRP131
A	GLU132
A	PRO134
A	ALA171
A	PHE179
A	GLN180
A	VAL183
A	HOH522

---

site_id	AC9
Number of Residues	7
Details	binding site for residue FMT B 401

Chain	Residue
B	HIS55
B	HIS57
B	LYS169
B	HIS201
B	HIS230
B	ZN402
B	ZN403

---

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN B 402

Chain	Residue
B	HIS55
B	HIS57
B	ASP301
B	FMT401

---

site_id	AD2
Number of Residues	3
Details	binding site for residue ZN B 403

Chain	Residue
B	HIS201
B	HIS230
B	FMT401

---

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	LYS169	metal ligand
A	HIS201	metal ligand
A	HIS230	metal ligand
A	ASP233	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLY254	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	ASP301	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	LYS169	metal ligand
B	HIS201	metal ligand
B	HIS230	metal ligand
B	ASP233	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLY254	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	ASP301	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

---