8P7N

The impact of molecular variants, crystallization conditions and space group on structure-ligand complexes: A case study on Bacterial Phosphotriesterase Variants and complexes

Replaces:  6FU0

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
C	0004063	molecular_function	aryldialkylphosphatase activity
C	0005886	cellular_component	plasma membrane
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	0005886	cellular_component	plasma membrane
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 PROSITE/UniProt

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

Chain	Residue	Details
A	GLY50-ILE58

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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

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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

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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

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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

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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

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site_id	MCSA3
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
C	HIS55	metal ligand
C	HIS57	metal ligand
C	LYS169	metal ligand
C	HIS201	metal ligand
C	HIS230	metal ligand
C	ASP233	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLY254	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	ASP301	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

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site_id	MCSA4
Number of Residues	8
Details	M-CSA 159

Chain	Residue	Details
D	HIS55	metal ligand
D	HIS57	metal ligand
D	LYS169	metal ligand
D	HIS201	metal ligand
D	HIS230	metal ligand
D	ASP233	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLY254	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	ASP301	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

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