Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TMY

Crystal structure of isoform CBd of the basic phospholipase A2 subunit of crotoxin from Crotalus durissus terrificus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004623	molecular_function	phospholipase A2 activity
A	0005509	molecular_function	calcium ion binding
A	0005543	molecular_function	phospholipid binding
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic process
A	0006644	biological_process	phospholipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0035821	biological_process	modulation of process of another organism
A	0042130	biological_process	negative regulation of T cell proliferation
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0050482	biological_process	arachidonate secretion
A	0090729	molecular_function	toxin activity
A	0099106	molecular_function	ion channel regulator activity
B	0004623	molecular_function	phospholipase A2 activity
B	0005509	molecular_function	calcium ion binding
B	0005543	molecular_function	phospholipid binding
B	0005576	cellular_component	extracellular region
B	0006629	biological_process	lipid metabolic process
B	0006644	biological_process	phospholipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0035821	biological_process	modulation of process of another organism
B	0042130	biological_process	negative regulation of T cell proliferation
B	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0050482	biological_process	arachidonate secretion
B	0090729	molecular_function	toxin activity
B	0099106	molecular_function	ion channel regulator activity
C	0004623	molecular_function	phospholipase A2 activity
C	0005509	molecular_function	calcium ion binding
C	0005543	molecular_function	phospholipid binding
C	0005576	cellular_component	extracellular region
C	0006629	biological_process	lipid metabolic process
C	0006644	biological_process	phospholipid metabolic process
C	0016042	biological_process	lipid catabolic process
C	0016787	molecular_function	hydrolase activity
C	0035821	biological_process	modulation of process of another organism
C	0042130	biological_process	negative regulation of T cell proliferation
C	0046872	molecular_function	metal ion binding
C	0047498	molecular_function	calcium-dependent phospholipase A2 activity
C	0050482	biological_process	arachidonate secretion
C	0090729	molecular_function	toxin activity
C	0099106	molecular_function	ion channel regulator activity
D	0004623	molecular_function	phospholipase A2 activity
D	0005509	molecular_function	calcium ion binding
D	0005543	molecular_function	phospholipid binding
D	0005576	cellular_component	extracellular region
D	0006629	biological_process	lipid metabolic process
D	0006644	biological_process	phospholipid metabolic process
D	0016042	biological_process	lipid catabolic process
D	0016787	molecular_function	hydrolase activity
D	0035821	biological_process	modulation of process of another organism
D	0042130	biological_process	negative regulation of T cell proliferation
D	0046872	molecular_function	metal ion binding
D	0047498	molecular_function	calcium-dependent phospholipase A2 activity
D	0050482	biological_process	arachidonate secretion
D	0090729	molecular_function	toxin activity
D	0099106	molecular_function	ion channel regulator activity
E	0004623	molecular_function	phospholipase A2 activity
E	0005509	molecular_function	calcium ion binding
E	0005543	molecular_function	phospholipid binding
E	0005576	cellular_component	extracellular region
E	0006629	biological_process	lipid metabolic process
E	0006644	biological_process	phospholipid metabolic process
E	0016042	biological_process	lipid catabolic process
E	0016787	molecular_function	hydrolase activity
E	0035821	biological_process	modulation of process of another organism
E	0042130	biological_process	negative regulation of T cell proliferation
E	0046872	molecular_function	metal ion binding
E	0047498	molecular_function	calcium-dependent phospholipase A2 activity
E	0050482	biological_process	arachidonate secretion
E	0090729	molecular_function	toxin activity
E	0099106	molecular_function	ion channel regulator activity
F	0004623	molecular_function	phospholipase A2 activity
F	0005509	molecular_function	calcium ion binding
F	0005543	molecular_function	phospholipid binding
F	0005576	cellular_component	extracellular region
F	0006629	biological_process	lipid metabolic process
F	0006644	biological_process	phospholipid metabolic process
F	0016042	biological_process	lipid catabolic process
F	0016787	molecular_function	hydrolase activity
F	0035821	biological_process	modulation of process of another organism
F	0042130	biological_process	negative regulation of T cell proliferation
F	0046872	molecular_function	metal ion binding
F	0047498	molecular_function	calcium-dependent phospholipase A2 activity
F	0050482	biological_process	arachidonate secretion
F	0090729	molecular_function	toxin activity
F	0099106	molecular_function	ion channel regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue NA A 201

Chain	Residue
A	TYR27
A	GLY29
A	GLY31
A	ASP48

site_id	AC2
Number of Residues	6
Details	binding site for residue PG4 A 202

Chain	Residue
A	HOH387
A	ASN6
A	ILE18
A	CYS28
A	GLY29
A	CYS44

site_id	AC3
Number of Residues	3
Details	binding site for residue PG4 A 203

Chain	Residue
A	LYS56
A	TRP80
A	CL206

site_id	AC4
Number of Residues	4
Details	binding site for residue CL A 204

Chain	Residue
A	ARG65
A	TYR66
B	ARG65
B	TYR66

site_id	AC5
Number of Residues	4
Details	binding site for residue CL A 205

Chain	Residue
A	HIS1
B	HIS1
B	HOH346
E	PRO19

site_id	AC6
Number of Residues	4
Details	binding site for residue CL A 206

Chain	Residue
A	TRP80
A	PG4203
A	HOH389
A	HOH457

site_id	AC7
Number of Residues	6
Details	binding site for residue NA A 207

Chain	Residue
A	PHE23
A	GLY25
A	TYR110
A	HOH307
A	HOH321
E	HOH400

site_id	AC8
Number of Residues	4
Details	binding site for residue NA B 201

Chain	Residue
B	TYR27
B	GLY29
B	GLY31
B	ASP48

site_id	AC9
Number of Residues	8
Details	binding site for residue PG4 B 202

Chain	Residue
B	PHE5
B	ASN6
B	TYR21
B	ALA22
B	CYS28
B	GLY29
B	CYS44
B	PG4203

site_id	AD1
Number of Residues	8
Details	binding site for residue PG4 B 203

Chain	Residue
B	LEU3
B	ILE18
B	PG4202
B	HOH347
B	HOH350
B	HOH381
E	TYR105
E	HOH338

site_id	AD2
Number of Residues	6
Details	binding site for residue NA B 204

Chain	Residue
B	PHE23
B	GLY25
B	TYR110
B	HOH335
B	HOH355
B	HOH398

site_id	AD3
Number of Residues	4
Details	binding site for residue NA C 201

Chain	Residue
C	TYR27
C	GLY29
C	GLY31
C	ASP48

site_id	AD4
Number of Residues	7
Details	binding site for residue PG4 C 202

Chain	Residue
C	PHE5
C	ASN6
C	TYR21
C	GLY29
C	CYS44
C	PG4203
C	HOH317

site_id	AD5
Number of Residues	6
Details	binding site for residue PG4 C 203

Chain	Residue
A	TYR105
A	HOH372
C	LEU2
C	TRP30
C	PG4202
C	HOH325

site_id	AD6
Number of Residues	7
Details	binding site for residue PG4 C 204

Chain	Residue
A	SER101
C	SER70
C	TYR72
C	ILE73
C	ARG90
C	HOH314
C	HOH328

site_id	AD7
Number of Residues	6
Details	binding site for residue CL C 205

Chain	Residue
C	ARG65
C	TYR66
C	HOH373
E	ARG65
E	TYR66
E	HOH347

site_id	AD8
Number of Residues	5
Details	binding site for residue NA C 206

Chain	Residue
C	PHE23
C	GLY25
C	TYR110
C	HOH306
C	HOH340

site_id	AD9
Number of Residues	6
Details	binding site for residue NA D 201

Chain	Residue
D	TYR27
D	GLY29
D	GLY31
D	ASP48
D	PG4202
D	HOH313

site_id	AE1
Number of Residues	12
Details	binding site for residue PG4 D 202

Chain	Residue
D	ASN6
D	ILE18
D	ALA22
D	TYR27
D	GLY29
D	CYS44
D	HIS47
D	ASP48
D	NA201
D	HOH317
D	HOH380
D	PHE5

site_id	AE2
Number of Residues	1
Details	binding site for residue CL D 203

Chain	Residue
D	HIS1

site_id	AE3
Number of Residues	4
Details	binding site for residue NA D 204

Chain	Residue
D	GLY25
D	ASP112
D	HOH302
D	HOH322

site_id	AE4
Number of Residues	8
Details	binding site for residue PG4 E 201

Chain	Residue
D	PHE11
D	GLU12
D	ARG14
D	ARG97
E	PHE11
E	ARG14
E	HOH336
E	HOH362

site_id	AE5
Number of Residues	4
Details	binding site for residue NA E 202

Chain	Residue
E	TYR27
E	GLY29
E	GLY31
E	ASP48

site_id	AE6
Number of Residues	6
Details	binding site for residue PG4 E 203

Chain	Residue
E	ASN6
E	ILE18
E	CYS28
E	GLY29
E	CYS44
E	HOH395

site_id	AE7
Number of Residues	4
Details	binding site for residue CL E 204

Chain	Residue
A	PRO19
C	HIS1
C	HOH336
E	HIS1

site_id	AE8
Number of Residues	7
Details	binding site for residue NA E 205

Chain	Residue
E	PHE23
E	GLY25
E	TYR110
E	HOH301
E	HOH304
E	HOH324
E	HOH396

site_id	AE9
Number of Residues	4
Details	binding site for residue NA F 201

Chain	Residue
F	TYR27
F	GLY29
F	GLY31
F	ASP48

site_id	AF1
Number of Residues	8
Details	binding site for residue PG4 F 202

Chain	Residue
F	LEU2
F	ASN6
F	ILE9
F	GLY29
F	CYS44
F	PG4203
F	HOH308
F	HOH357

site_id	AF2
Number of Residues	6
Details	binding site for residue PG4 F 203

Chain	Residue
D	TYR105
F	LEU2
F	LEU3
F	PG4202
F	HOH357
F	HOH358

site_id	AF3
Number of Residues	4
Details	binding site for residue PG4 F 204

Chain	Residue
F	SER67
F	LYS69
F	SER70
F	TYR72

site_id	AF4
Number of Residues	2
Details	binding site for residue CL F 205

Chain	Residue
F	ARG65
F	TYR66

site_id	AF5
Number of Residues	5
Details	binding site for residue NA F 206

Chain	Residue
F	PHE23
F	GLY25
F	TYR110
F	HOH302
F	HOH394

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS43-CYS50

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

Chain	Residue	Details
A	ILE85-CYS95

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"18275084","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18275084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Site: {"description":"Responsible for the weak stability and toxicity","evidences":[{"source":"PubMed","id":"21787789","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	54
Details	Site: {"description":"Putative interfacial binding surface (IBS)","evidences":[{"source":"PubMed","id":"21787789","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Site: {"description":"Responsible for the higher anticoagulant activity (compared with CBa2)","evidences":[{"source":"PubMed","id":"18062812","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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