Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5WCQ

Phosphotriesterase variant S2

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
G	0004063	molecular_function	aryldialkylphosphatase activity
G	0005886	cellular_component	plasma membrane
G	0008270	molecular_function	zinc ion binding
G	0009056	biological_process	catabolic process
G	0016787	molecular_function	hydrolase activity
G	0016788	molecular_function	hydrolase activity, acting on ester bonds
G	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 2401

Chain	Residue
A	HIS55
A	HIS57
A	KCX169
A	ASP301
A	CAC2403

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 2402

Chain	Residue
A	KCX169
A	HIS201
A	HIS230
A	CAC2403

site_id	AC3
Number of Residues	10
Details	binding site for residue CAC A 2403

Chain	Residue
A	HIS55
A	HIS57
A	TRP131
A	KCX169
A	HIS201
A	HIS230
A	ASP301
A	ZN2401
A	ZN2402
A	MPD2406

site_id	AC4
Number of Residues	4
Details	binding site for residue MPD A 2404

Chain	Residue
A	ARG337
A	GLN343
A	LEU346
A	HOH2617

site_id	AC5
Number of Residues	5
Details	binding site for residue MPD A 2405

Chain	Residue
A	ARG41
A	GLY42
A	THR161
A	GLY162
A	HOH2628

site_id	AC6
Number of Residues	5
Details	binding site for residue MPD A 2406

Chain	Residue
A	TRP131
A	ILE306
A	SER308
A	CAC2403
A	HOH2502

site_id	AC7
Number of Residues	5
Details	binding site for residue MPD A 2407

Chain	Residue
A	ARG41
A	ARG118
A	ARG207
A	ASP236
A	HOH2523

site_id	AC8
Number of Residues	5
Details	binding site for residue ZN G 2401

Chain	Residue
G	HIS55
G	HIS57
G	KCX169
G	ASP301
G	CAC2403

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN G 2402

Chain	Residue
G	KCX169
G	HIS201
G	HIS230
G	CAC2403

site_id	AD1
Number of Residues	10
Details	binding site for residue CAC G 2403

Chain	Residue
G	HIS55
G	HIS57
G	TRP131
G	KCX169
G	HIS201
G	HIS230
G	ASP301
G	ZN2401
G	ZN2402
G	MPD2406

site_id	AD2
Number of Residues	3
Details	binding site for residue MPD G 2404

Chain	Residue
G	PHE51
G	ARG337
G	GLN343

site_id	AD3
Number of Residues	10
Details	binding site for residue MPD G 2405

Chain	Residue
G	GLU81
G	VAL84
G	ARG88
G	GLU115
G	ALA119
G	GLU217
G	HOH2538
G	HOH2545
G	HOH2640
G	HOH2652

site_id	AD4
Number of Residues	6
Details	binding site for residue MPD G 2406

Chain	Residue
G	TRP131
G	LEU271
G	SER308
G	TYR309
G	CAC2403
G	HOH2699

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

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