1MDU

Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0051015	molecular_function	actin filament binding
B	0001725	cellular_component	stress fiber
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0016787	molecular_function	hydrolase activity
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0048741	biological_process	skeletal muscle fiber development
D	0051015	molecular_function	actin filament binding
E	0001725	cellular_component	stress fiber
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0016787	molecular_function	hydrolase activity
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0048741	biological_process	skeletal muscle fiber development

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 401

Chain	Residue
B	ATP400
B	HOH405
B	HOH406
B	HOH407
B	HOH408
B	HOH409

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 402

Chain	Residue
A	VAL121
A	HOH513
A	GLY41
A	ASP42
A	GLU73

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 403

Chain	Residue
A	ASP85
A	GLY90
A	ALA92
A	HOH486
A	HOH505
B	GLU169
B	HOH413

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 404

Chain	Residue
B	SER325
B	HOH471
B	HOH472
B	HOH531
B	HOH572
D	GLU14

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 401

Chain	Residue
E	ATP400
E	HOH408
E	HOH410
E	HOH411
E	HOH480

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 402

Chain	Residue
D	GLY41
D	ASP42
D	GLU73
D	VAL121
D	HOH418
D	HOH455

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 403

Chain	Residue
D	ASP85
D	GLY90
D	ALA92
D	HOH425
E	GLU169
E	HOH403

---

site_id	AC8
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ATP B 400

Chain	Residue
B	GLY15
B	SER16
B	GLY17
B	LEU18
B	LYS20
B	GLY158
B	ASP159
B	GLY160
B	VAL161
B	ARG212
B	LYS215
B	GLU216
B	GLY303
B	GLY304
B	THR305
B	MET307
B	TYR308
B	LYS338
B	CA401
B	HOH408
B	HOH409
B	HOH410
B	HOH411
B	HOH412
B	HOH478
B	HOH507
B	HOH551

---

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP E 400

Chain	Residue
E	GLY15
E	SER16
E	GLY17
E	LEU18
E	LYS20
E	GLY158
E	ASP159
E	GLY160
E	VAL161
E	GLY184
E	LYS215
E	GLU216
E	GLY303
E	GLY304
E	THR305
E	MET307
E	TYR308
E	LYS338
E	CA401
E	HOH408
E	HOH410
E	HOH412
E	HOH433
E	HOH484

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 472

Chain	Residue
A	TYR35
A	TYR109
A	PHE110
A	LYS111
A	SER112
E	ASN227
E	HOH454

---

Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
B	TYR55-GLY65

---

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WITKqEYDE

Chain	Residue	Details
B	TRP358-GLU366

---

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
B	LEU106-ARG118

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737

Chain	Residue	Details
A	GLU73
A	ASP85
A	GLY90
A	ALA92
A	VAL121
D	GLY41
D	ASP42
D	GLU73
D	ASP85
D	GLY90
D	ALA92
D	VAL121
B	CYS2
E	CYS2

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:456601

Chain	Residue	Details
B	ASP3
E	ASP3

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134

Chain	Residue	Details
B	MET46
B	MET49
E	MET46
E	MET49

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU

Chain	Residue	Details
B	HIC75
E	HIC75

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133

Chain	Residue	Details
B	LYS86
E	LYS86

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