1D0N

THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003779	molecular_function	actin binding
A	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0007015	biological_process	actin filament organization
A	0007417	biological_process	central nervous system development
A	0008154	biological_process	actin polymerization or depolymerization
A	0015629	cellular_component	actin cytoskeleton
A	0030030	biological_process	cell projection organization
A	0030031	biological_process	cell projection assembly
A	0046872	molecular_function	metal ion binding
A	0051014	biological_process	actin filament severing
A	0051015	molecular_function	actin filament binding
A	0051016	biological_process	barbed-end actin filament capping
A	0051693	biological_process	actin filament capping
A	0060271	biological_process	cilium assembly
B	0003779	molecular_function	actin binding
B	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0007015	biological_process	actin filament organization
B	0007417	biological_process	central nervous system development
B	0008154	biological_process	actin polymerization or depolymerization
B	0015629	cellular_component	actin cytoskeleton
B	0030030	biological_process	cell projection organization
B	0030031	biological_process	cell projection assembly
B	0046872	molecular_function	metal ion binding
B	0051014	biological_process	actin filament severing
B	0051015	molecular_function	actin filament binding
B	0051016	biological_process	barbed-end actin filament capping
B	0051693	biological_process	actin filament capping
B	0060271	biological_process	cilium assembly

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI

Chain	Residue	Details
A	ASP66
A	ARG328
B	ASP66
B	ALA67
B	SER98
B	ASP110
B	ARG115
B	VAL117
B	ALA146
B	ASP303
B	CYS304
A	ALA67
B	ARG328
A	SER98
A	ASP110
A	ARG115
A	VAL117
A	ALA146
A	ASP303
A	CYS304

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER136
A	LEU162
B	SER136
B	LEU162

---

site_id	SWS_FT_FI3
Number of Residues	34
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P06396

Chain	Residue	Details
A	ASP187
A	VAL495
A	SER525
A	ASP565
A	ALA566
A	LYS588
A	ASP670
A	VAL671
A	LYS693
B	ASP187
B	CYS188
A	CYS188
B	ARG210
B	THR260
B	ASP445
B	SER446
B	VAL476
B	GLU488
B	THR493
B	VAL495
B	SER525
B	ASP565
A	ARG210
B	ALA566
B	LYS588
B	ASP670
B	VAL671
B	LYS693
A	THR260
A	ASP445
A	SER446
A	VAL476
A	GLU488
A	THR493

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06396

Chain	Residue	Details
A	GLY60
B	ARG625
A	LEU383
A	GLY439
A	LEU577
A	ARG625
B	GLY60
B	LEU383
B	GLY439
B	LEU577

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13020

Chain	Residue	Details
A	ALA558
B	ALA558

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P06396

Chain	Residue	Details
A	PRO716
B	PRO716

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