Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3BJW

Crystal Structure of ecarpholin S complexed with suramin

Replaces: 2QHG

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	0006644	biological_process	phospholipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0042130	biological_process	negative regulation of T cell proliferation
A	0050482	biological_process	arachidonate secretion
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	0006644	biological_process	phospholipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0042130	biological_process	negative regulation of T cell proliferation
B	0050482	biological_process	arachidonate secretion
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	0006644	biological_process	phospholipid metabolic process
C	0016042	biological_process	lipid catabolic process
C	0042130	biological_process	negative regulation of T cell proliferation
C	0050482	biological_process	arachidonate secretion
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	0006644	biological_process	phospholipid metabolic process
D	0016042	biological_process	lipid catabolic process
D	0042130	biological_process	negative regulation of T cell proliferation
D	0050482	biological_process	arachidonate secretion
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	0006644	biological_process	phospholipid metabolic process
E	0016042	biological_process	lipid catabolic process
E	0042130	biological_process	negative regulation of T cell proliferation
E	0050482	biological_process	arachidonate secretion
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	0006644	biological_process	phospholipid metabolic process
F	0016042	biological_process	lipid catabolic process
F	0042130	biological_process	negative regulation of T cell proliferation
F	0050482	biological_process	arachidonate secretion
G	0004623	molecular_function	phospholipase A2 activity
G	0005509	molecular_function	calcium ion binding
G	0005543	molecular_function	phospholipid binding
G	0005576	cellular_component	extracellular region
G	0006644	biological_process	phospholipid metabolic process
G	0016042	biological_process	lipid catabolic process
G	0042130	biological_process	negative regulation of T cell proliferation
G	0050482	biological_process	arachidonate secretion
H	0004623	molecular_function	phospholipase A2 activity
H	0005509	molecular_function	calcium ion binding
H	0005543	molecular_function	phospholipid binding
H	0005576	cellular_component	extracellular region
H	0006644	biological_process	phospholipid metabolic process
H	0016042	biological_process	lipid catabolic process
H	0042130	biological_process	negative regulation of T cell proliferation
H	0050482	biological_process	arachidonate secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SVR A 508

Chain	Residue
A	PRO36
E	GLN11
E	ARG77
E	SVR503
E	SVR510
G	VAL2
G	VAL3
G	GLY6
G	ARG72
G	HOH511
H	PHE124
A	PHE124
A	TRP125
A	LYS127
A	GLY128
A	HOH522
A	HOH527
A	HOH536
E	VAL3

site_id	AC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE SVR B 501

Chain	Residue
A	SER17
A	PRO18
A	PHE19
A	PRO20
B	VAL2
B	VAL3
B	LEU5
B	GLY6
B	ILE10
B	LYS16
B	SER17
B	PRO18
B	PHE19
B	PRO20
B	SER21
B	THR23
B	LYS115
B	SVR512
B	HOH522
B	HOH541
B	HOH556
B	HOH563
F	LYS116
F	ASN122
F	PHE124
G	LYS116
G	SVR506
G	HOH515

site_id	AC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE SVR B 512

Chain	Residue
A	VAL2
A	VAL3
A	THR70
A	ARG72
B	VAL3
B	LYS7
B	ILE10
B	GLN11
B	GLU12
B	THR13
B	GLY14
B	ARG107
B	LEU110
B	SVR501
B	HOH517
B	HOH518
B	HOH539
B	HOH547
G	LYS16
G	TYR113
G	ASN114
G	LYS115
G	LYS116
G	TYR117
G	TRP125
G	SVR506
G	HOH538
G	HOH541

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE SVR C 505

Chain	Residue
C	PRO36
C	PHE124
C	TRP125
C	LYS127
C	GLY128
C	HOH522
C	HOH551
D	VAL2
D	VAL3
D	GLY6
D	LYS7
D	LYS69
D	ARG72
D	HOH146
D	HOH161
E	PHE124
H	VAL2
H	VAL3
H	GLN11
H	PHE19
H	ARG77
H	SVR504
H	SVR511

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE SVR C 507

Chain	Residue
C	VAL2
C	VAL3
C	GLY6
C	PRO18
C	LYS69
C	ARG72
C	HOH508
C	HOH515
C	HOH524
C	HOH527
C	HOH549
D	PRO36
D	PHE124
D	LYS127
F	VAL3
F	GLN11
F	ARG77
F	SVR502
F	SVR509
F	HOH519
B	PHE124

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE SVR E 503

Chain	Residue
A	LYS116
A	SVR508
E	VAL2
E	VAL3
E	LEU5
E	GLY6
E	ILE10
E	LYS16
E	SER17
E	PRO18
E	PHE19
E	PRO20
E	SER21
E	THR23
E	LYS115
E	SVR510
E	HOH513
E	HOH530
E	HOH537
G	SER17
G	PRO18
G	PHE19
G	PRO20
H	LYS116
H	ASN122
H	PHE124

site_id	AC7
Number of Residues	25
Details	BINDING SITE FOR RESIDUE SVR E 510

Chain	Residue
A	LYS16
A	TYR113
A	ASN114
A	LYS115
A	TYR117
A	TRP125
A	SVR508
A	HOH524
A	HOH530
E	VAL3
E	LYS7
E	ILE10
E	GLN11
E	GLU12
E	THR13
E	GLY14
E	ARG107
E	LEU110
E	ASN111
E	SVR503
E	HOH541
G	VAL2
G	VAL3
G	THR70
G	ARG72

site_id	AC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE SVR F 502

Chain	Residue
B	LYS116
B	ASN122
B	PHE124
C	SER17
C	PHE19
C	PRO20
C	SVR507
D	LYS116
D	HOH140
F	VAL2
F	LEU5
F	GLY6
F	ILE10
F	LYS16
F	SER17
F	PRO18
F	PRO20
F	SER21
F	THR23
F	LYS115
F	SVR509
F	HOH512
F	HOH527
F	HOH554

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE SVR F 509

Chain	Residue
C	VAL2
C	VAL3
C	THR23
C	THR70
C	SVR507
D	LYS16
D	TYR113
D	ASN114
D	LYS115
D	PRO121
D	PHE124
D	TRP125
F	VAL3
F	LYS7
F	ILE10
F	GLN11
F	GLU12
F	THR13
F	GLY14
F	ARG107
F	LEU110
F	SVR502
F	HOH520
F	HOH551

site_id	BC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE SVR G 506

Chain	Residue
A	VAL2
A	VAL3
A	GLY6
A	LYS7
A	ARG72
A	LYS74
A	HOH509
B	VAL2
B	VAL3
B	GLN11
B	ARG77
B	SVR501
B	SVR512
B	HOH518
F	PHE124
F	TRP125
F	HOH507
G	PRO36
G	PHE124
G	TRP125
G	LYS127
G	GLY128
G	HOH521
G	HOH522
G	HOH528
G	HOH531
G	HOH536
G	HOH540
G	HOH541

site_id	BC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE SVR H 504

Chain	Residue
C	LYS116
C	SVR505
C	HOH512
D	SER17
D	PRO18
D	PHE19
D	PRO20
E	PRO121
E	ASN122
E	PHE124
H	VAL2
H	LEU5
H	GLY6
H	ILE10
H	LYS16
H	SER17
H	PRO18
H	PHE19
H	PRO20
H	SER21
H	THR23
H	LYS115
H	SVR511
H	HOH518
H	HOH530

site_id	BC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE SVR H 511

Chain	Residue
C	LYS16
C	TYR113
C	ASN114
C	LYS115
C	LYS116
C	TYR117
C	TRP125
C	SVR505
D	VAL2
D	VAL3
D	THR70
D	ARG72
D	HOH151
H	LYS7
H	ILE10
H	GLN11
H	GLU12
H	THR13
H	GLY14
H	ARG107
H	LEU110
H	SVR504
H	HOH525
H	HOH537

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS44-CYS51

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

Chain	Residue	Details
A	ILE95-CYS105

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	96
Details	Region: {"description":"Important for membrane-damaging activities in eukaryotes and bacteria; heparin-binding","evidences":[{"source":"UniProtKB","id":"P24605","evidenceCode":"ECO:0000250"}]}

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

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
G	HIS48
G	GLY30
G	ASP99

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
H	HIS48
H	GLY30
H	ASP99

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