Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1M8T

Structure of an acidic Phospholipase A2 from the venom of Ophiophagus hannah at 2.1 resolution from a hemihedrally twinned crystal form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004623	molecular_function	A2-type glycerophospholipase activity
A	0005102	molecular_function	signaling receptor binding
A	0005509	molecular_function	calcium ion binding
A	0005543	molecular_function	phospholipid binding
A	0005576	cellular_component	extracellular region
A	0006633	biological_process	fatty acid biosynthetic process
A	0006644	biological_process	phospholipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0048146	biological_process	positive regulation of fibroblast proliferation
A	0050482	biological_process	arachidonate secretion
B	0004623	molecular_function	A2-type glycerophospholipase activity
B	0005102	molecular_function	signaling receptor binding
B	0005509	molecular_function	calcium ion binding
B	0005543	molecular_function	phospholipid binding
B	0005576	cellular_component	extracellular region
B	0006633	biological_process	fatty acid biosynthetic process
B	0006644	biological_process	phospholipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0048146	biological_process	positive regulation of fibroblast proliferation
B	0050482	biological_process	arachidonate secretion
C	0004623	molecular_function	A2-type glycerophospholipase activity
C	0005102	molecular_function	signaling receptor binding
C	0005509	molecular_function	calcium ion binding
C	0005543	molecular_function	phospholipid binding
C	0005576	cellular_component	extracellular region
C	0006633	biological_process	fatty acid biosynthetic process
C	0006644	biological_process	phospholipid metabolic process
C	0016042	biological_process	lipid catabolic process
C	0048146	biological_process	positive regulation of fibroblast proliferation
C	0050482	biological_process	arachidonate secretion
D	0004623	molecular_function	A2-type glycerophospholipase activity
D	0005102	molecular_function	signaling receptor binding
D	0005509	molecular_function	calcium ion binding
D	0005543	molecular_function	phospholipid binding
D	0005576	cellular_component	extracellular region
D	0006633	biological_process	fatty acid biosynthetic process
D	0006644	biological_process	phospholipid metabolic process
D	0016042	biological_process	lipid catabolic process
D	0048146	biological_process	positive regulation of fibroblast proliferation
D	0050482	biological_process	arachidonate secretion
E	0004623	molecular_function	A2-type glycerophospholipase activity
E	0005102	molecular_function	signaling receptor binding
E	0005509	molecular_function	calcium ion binding
E	0005543	molecular_function	phospholipid binding
E	0005576	cellular_component	extracellular region
E	0006633	biological_process	fatty acid biosynthetic process
E	0006644	biological_process	phospholipid metabolic process
E	0016042	biological_process	lipid catabolic process
E	0048146	biological_process	positive regulation of fibroblast proliferation
E	0050482	biological_process	arachidonate secretion
F	0004623	molecular_function	A2-type glycerophospholipase activity
F	0005102	molecular_function	signaling receptor binding
F	0005509	molecular_function	calcium ion binding
F	0005543	molecular_function	phospholipid binding
F	0005576	cellular_component	extracellular region
F	0006633	biological_process	fatty acid biosynthetic process
F	0006644	biological_process	phospholipid metabolic process
F	0016042	biological_process	lipid catabolic process
F	0048146	biological_process	positive regulation of fibroblast proliferation
F	0050482	biological_process	arachidonate secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1001

Chain	Residue
A	TYR28
A	GLY30
A	GLY32
A	ASP49
A	HOH1020
A	HOH1077

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1002

Chain	Residue
B	ASP49
B	HOH1140
B	HOH1164
B	TYR28
B	GLY30
B	GLY32

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 1003

Chain	Residue
C	TYR28
C	GLY30
C	GLY32
C	ASP49
C	HOH1073

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 1004

Chain	Residue
D	TYR28
D	GLY30
D	GLY32
D	ASP49
D	HEZ1009
D	HOH1025

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 1005

Chain	Residue
E	TYR28
E	GLY30
E	GLY32
E	ASP49
E	HOH1036
E	HOH1103

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA F 1006

Chain	Residue
F	TYR28
F	GLY30
F	GLY32
F	ASP49

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HEZ A 1002

Chain	Residue
A	LEU2
A	VAL3
A	ARG10

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HEZ A 1004

Chain	Residue
A	ASP76
A	SER78
A	GLU79

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE HEZ C 1005

Chain	Residue
C	TRP19

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HEZ C 1006

Chain	Residue
C	LEU2
C	VAL3
C	ASN6
C	TRP19

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HEZ D 1008

Chain	Residue
D	TRP19
D	SER23
D	HEZ1009
D	HOH1102

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE HEZ D 1009

Chain	Residue
D	LEU2
D	ASN6
D	TYR22
D	CYS29
D	GLY30
D	CA1004
D	HEZ1008
D	HOH1031

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HEZ D 1010

Chain	Residue
D	LEU2
D	VAL3
D	ASN6
D	TRP19

Functional Information from PROSITE/UniProt

site_id	PS00118
Number of Residues	8
Details	PA2_HIS Phospholipase A2 histidine active site. CCQvHDnC

Chain	Residue	Details
A	CYS44-CYS51

site_id	PS00119
Number of Residues	11
Details	PA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRVAaIC

Chain	Residue	Details
A	VAL95-CYS105

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12925787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1M8T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
A	HIS48
A	GLY30
A	ASP99

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
B	HIS48
B	GLY30
B	ASP99

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
C	HIS48
C	GLY30
C	ASP99

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
D	HIS48
D	GLY30
D	ASP99

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
E	HIS48
E	GLY30
E	ASP99

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
F	HIS48
F	GLY30
F	ASP99

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