Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VC5

Structural basis for natural lactonase and promiscuous phosphotriesterase activities

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004063	molecular_function	aryldialkylphosphatase activity
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	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
C	0004063	molecular_function	aryldialkylphosphatase activity
C	0008270	molecular_function	zinc ion binding
C	0009056	biological_process	catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016788	molecular_function	hydrolase activity, acting on ester bonds
C	0046872	molecular_function	metal ion binding
D	0004063	molecular_function	aryldialkylphosphatase activity
D	0008270	molecular_function	zinc ion binding
D	0009056	biological_process	catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016788	molecular_function	hydrolase activity, acting on ester bonds
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE A1315

Chain	Residue
A	HIS22
A	HIS24
A	KCX137
A	ASP256
A	CO1316
A	HOH2064

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO A1316

Chain	Residue
A	ARG223
A	FE21315
A	HOH2064
A	KCX137
A	HIS170
A	HIS199

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE B1315

Chain	Residue
B	HIS22
B	HIS24
B	KCX137
B	ASP256
B	CO1316
B	HOH2062

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO B1316

Chain	Residue
B	KCX137
B	HIS170
B	HIS199
B	ARG223
B	FE21315
B	HOH2062

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE C1315

Chain	Residue
C	HIS22
C	HIS24
C	KCX137
C	ASP256
C	CO1316
C	HOH2056

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CO C1316

Chain	Residue
C	KCX137
C	HIS170
C	HIS199
C	ARG223
C	FE21315
C	HOH2013
C	HOH2056

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE D1315

Chain	Residue
D	HIS22
D	HIS24
D	KCX137
D	ASP256
D	CO1316
D	HOH2061

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO D1316

Chain	Residue
D	KCX137
D	HIS170
D	HIS199
D	ARG223
D	FE21315
D	HOH2061

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A1317

Chain	Residue
A	TYR99
A	ILE100
A	ASP101
B	PHE104
B	EDO1321

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D1317

Chain	Residue
D	ASN172
D	ALA173
D	HIS174
D	ASP202
D	PHE229
D	HOH2045

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C1317

Chain	Residue
C	ASN160
C	LYS164
C	GLY189
C	ASP191

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D1318

Chain	Residue
C	PHE104
D	TYR99
D	ILE100
D	ASP101

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B1317

Chain	Residue
B	TYR257
B	CYS258
B	ILE261
B	ALA266
B	LYS271

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A1318

Chain	Residue
A	ASN160
A	LYS164
A	GLY189
A	ASP191
A	LYS194

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B1318

Chain	Residue
B	ASN160
B	LYS164
B	GLY189
B	VAL190
B	ASP191

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D1319

Chain	Residue
D	ASN160
D	LYS164
D	GLY189
D	VAL190
D	ASP191

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B1319

Chain	Residue
B	SER171
B	ASN172
B	ALA173
B	ASP202
B	ARG223
B	PHE229

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B1320

Chain	Residue
B	EDO1321
A	PHE104
B	ILE98
B	TYR99
B	ILE100
B	ASP101

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A1319

Chain	Residue
A	LYS14
A	GLY17

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO D1320

Chain	Residue
D	GLY128
D	THR129

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A1320

Chain	Residue
A	LEU5
A	ASP9
A	SER10
A	ASN131
A	LYS132

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B1321

Chain	Residue
A	EDO1317
B	ASP101
B	LEU102
B	PHE104
B	GOL1320
B	EDO1323

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C1318

Chain	Residue
C	LEU39
C	ILE261

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO B1322

Chain	Residue
B	ALA266
B	TRP278

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B1323

Chain	Residue
B	LEU102
B	PRO103
B	LEU107
B	ASP148
B	EDO1321

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A1321

Chain	Residue
A	ASP141
A	SER171
A	ASN172
A	ALA173
A	ASP202
A	ARG223
A	PHE229

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C1319

Chain	Residue
C	TYR99
C	ILE100
C	ASP101
D	PHE104

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B1324

Chain	Residue
A	SER29
A	GLY71
B	PRO103
B	PHE104

site_id	DC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO D1321

Chain	Residue
D	ALA266

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY17-LEU25

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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