Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3CS2

Crystal structure of PTE G60A mutant

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
K	0004063	molecular_function	aryldialkylphosphatase activity
K	0005886	cellular_component	plasma membrane
K	0008270	molecular_function	zinc ion binding
K	0009056	biological_process	catabolic process
K	0016020	cellular_component	membrane
K	0016787	molecular_function	hydrolase activity
K	0016788	molecular_function	hydrolase activity, acting on ester bonds
K	0046872	molecular_function	metal ion binding
P	0004063	molecular_function	aryldialkylphosphatase activity
P	0005886	cellular_component	plasma membrane
P	0008270	molecular_function	zinc ion binding
P	0009056	biological_process	catabolic process
P	0016020	cellular_component	membrane
P	0016787	molecular_function	hydrolase activity
P	0016788	molecular_function	hydrolase activity, acting on ester bonds
P	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CAC A 1

Chain	Residue
A	HIS57
A	ILE106
A	TRP131
A	HIS201
A	ASP301

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CAC B 2

Chain	Residue
B	ASP301
B	HIS57
B	ILE106
B	TRP131
B	HIS201

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CAC K 3

Chain	Residue
K	HIS57
K	ILE106
K	TRP131
K	HIS201
K	ASP301

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CAC P 4

Chain	Residue
P	HIS57
P	ILE106
P	TRP131
P	HIS201
P	ASP301

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CO A 365

Chain	Residue
A	HIS55
A	HIS57
A	ASP301

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CO A 2

Chain	Residue
A	HIS201
A	HIS230

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CO B 3

Chain	Residue
B	HIS55
B	HIS57
B	ASP301

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CO B 4

Chain	Residue
B	HIS201
B	HIS230

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CO K 5

Chain	Residue
K	HIS55
K	HIS57
K	ASP301

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CO K 6

Chain	Residue
K	HIS201
K	HIS230

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CO P 7

Chain	Residue
P	HIS55
P	HIS57
P	ASP301

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CO P 8

Chain	Residue
P	HIS201
P	HIS230

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	20
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	4
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	4
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	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
A	HIS254
A	ASP233
A	ASP301

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
B	HIS254
B	ASP233
B	ASP301

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
K	HIS254
K	ASP233
K	ASP301

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ez2

Chain	Residue	Details
P	HIS254
P	ASP233
P	ASP301

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