Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5IZR

Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate inhibitor and Terbium Chloride

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004620	molecular_function	glycerophospholipase activity
A	0004623	molecular_function	A2-type glycerophospholipase activity
A	0005509	molecular_function	calcium ion binding
A	0005544	molecular_function	calcium-dependent phospholipid binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006650	biological_process	glycerophospholipid metabolic process
A	0008970	molecular_function	glycerophospholipid phospholipase A1 activity
A	0009395	biological_process	phospholipid catabolic process
A	0016020	cellular_component	membrane
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0036148	biological_process	phosphatidylglycerol acyl-chain remodeling
A	0036149	biological_process	phosphatidylinositol acyl-chain remodeling
A	0046475	biological_process	glycerophospholipid catabolic process
A	0046872	molecular_function	metal ion binding
B	0004620	molecular_function	glycerophospholipase activity
B	0004623	molecular_function	A2-type glycerophospholipase activity
B	0005509	molecular_function	calcium ion binding
B	0005544	molecular_function	calcium-dependent phospholipid binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006650	biological_process	glycerophospholipid metabolic process
B	0008970	molecular_function	glycerophospholipid phospholipase A1 activity
B	0009395	biological_process	phospholipid catabolic process
B	0016020	cellular_component	membrane
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0036148	biological_process	phosphatidylglycerol acyl-chain remodeling
B	0036149	biological_process	phosphatidylinositol acyl-chain remodeling
B	0046475	biological_process	glycerophospholipid catabolic process
B	0046872	molecular_function	metal ion binding
C	0004620	molecular_function	glycerophospholipase activity
C	0004623	molecular_function	A2-type glycerophospholipase activity
C	0005509	molecular_function	calcium ion binding
C	0005544	molecular_function	calcium-dependent phospholipid binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006650	biological_process	glycerophospholipid metabolic process
C	0008970	molecular_function	glycerophospholipid phospholipase A1 activity
C	0009395	biological_process	phospholipid catabolic process
C	0016020	cellular_component	membrane
C	0016042	biological_process	lipid catabolic process
C	0016787	molecular_function	hydrolase activity
C	0036148	biological_process	phosphatidylglycerol acyl-chain remodeling
C	0036149	biological_process	phosphatidylinositol acyl-chain remodeling
C	0046475	biological_process	glycerophospholipid catabolic process
C	0046872	molecular_function	metal ion binding
D	0004620	molecular_function	glycerophospholipase activity
D	0004623	molecular_function	A2-type glycerophospholipase activity
D	0005509	molecular_function	calcium ion binding
D	0005544	molecular_function	calcium-dependent phospholipid binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006650	biological_process	glycerophospholipid metabolic process
D	0008970	molecular_function	glycerophospholipid phospholipase A1 activity
D	0009395	biological_process	phospholipid catabolic process
D	0016020	cellular_component	membrane
D	0016042	biological_process	lipid catabolic process
D	0016787	molecular_function	hydrolase activity
D	0036148	biological_process	phosphatidylglycerol acyl-chain remodeling
D	0036149	biological_process	phosphatidylinositol acyl-chain remodeling
D	0046475	biological_process	glycerophospholipid catabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue 7FA A 901

Chain	Residue
A	GLY330
A	TYR650
A	GLY331
A	SER361
A	GLY362
A	SER528
A	ILE530
A	PHE531
A	GLY582
A	LEU585

site_id	AC2
Number of Residues	5
Details	binding site for residue TB A 902

Chain	Residue
A	ASP44
A	ASP66
A	HOH1001
A	HOH1002
A	HOH1003

site_id	AC3
Number of Residues	2
Details	binding site for residue TB A 903

Chain	Residue
A	ASP96
A	ASP102

site_id	AC4
Number of Residues	1
Details	binding site for residue TB A 904

Chain	Residue
A	ASP101

site_id	AC5
Number of Residues	1
Details	binding site for residue TB A 905

Chain	Residue
A	ASP647

site_id	AC6
Number of Residues	2
Details	binding site for residue TB B 902

Chain	Residue
B	ASP44
B	ASP66

site_id	AC7
Number of Residues	1
Details	binding site for residue TB B 903

Chain	Residue
B	ASP102

site_id	AC8
Number of Residues	1
Details	binding site for residue TB B 904

Chain	Residue
B	ASP101

site_id	AC9
Number of Residues	1
Details	binding site for residue TB B 905

Chain	Residue
B	ASP647

site_id	AD1
Number of Residues	3
Details	binding site for residue TB C 902

Chain	Residue
C	ASP44
C	ASP66
C	HOH1002

site_id	AD2
Number of Residues	2
Details	binding site for residue TB C 903

Chain	Residue
C	ASP96
C	ASP102

site_id	AD3
Number of Residues	2
Details	binding site for residue TB C 904

Chain	Residue
C	THR99
C	ASP101

site_id	AD4
Number of Residues	3
Details	binding site for residue TB D 902

Chain	Residue
D	ASP44
D	ASP66
D	HOH1003

site_id	AD5
Number of Residues	1
Details	binding site for residue TB D 903

Chain	Residue
D	ASP102

site_id	AD6
Number of Residues	1
Details	binding site for residue TB D 904

Chain	Residue
D	ASP101

site_id	AD7
Number of Residues	1
Details	binding site for residue TB D 905

Chain	Residue
D	ASP647

site_id	AD8
Number of Residues	14
Details	binding site for Di-peptide 7FA B 901 and SER B 361

Chain	Residue
B	GLY330
B	GLY331
B	ILE360
B	GLY362
B	SER363
B	THR364
B	TRP365
B	TRP527
B	SER528
B	ILE530
B	GLY582
B	LEU585
B	TYR650
B	LEU768

site_id	AD9
Number of Residues	11
Details	binding site for Di-peptide 7FA C 901 and SER C 361

Chain	Residue
C	GLY330
C	GLY331
C	ILE360
C	GLY362
C	SER363
C	THR364
C	TRP365
C	TRP527
C	SER528
C	GLY582
C	TYR650

site_id	AE1
Number of Residues	13
Details	binding site for Di-peptide 7FA D 901 and SER D 361

Chain	Residue
D	GLY330
D	GLY331
D	ILE360
D	GLY362
D	SER363
D	THR364
D	TRP365
D	TRP527
D	SER528
D	ILE530
D	GLY582
D	LEU585
D	TYR650

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"27220631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IXC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IZR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P47712","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27220631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IXC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IZR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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