5SYG

Cryo-EM reconstruction of zampanolide-bound microtubule

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000278	biological_process	mitotic cell cycle
A	0003924	molecular_function	GTPase activity
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0007017	biological_process	microtubule-based process
A	0015630	cellular_component	microtubule cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0000226	biological_process	microtubule cytoskeleton organization
B	0000278	biological_process	mitotic cell cycle
B	0003924	molecular_function	GTPase activity
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005874	cellular_component	microtubule
B	0007017	biological_process	microtubule-based process
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	SER140
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	ILE171
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	GLN11
A	LEU227
A	ASN228
A	MG502
B	LEU248
B	LYS254
A	ALA12
A	GLN15
A	GLU71
A	ASP98
A	ALA99
A	ALA100
A	ASN101

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 502

Chain	Residue
A	GLN11
A	GLU71
A	GTP501

---

site_id	AC3
Number of Residues	15
Details	binding site for residue GDP B 501

Chain	Residue
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	ASN101
B	SER140
B	GLY143
B	GLY144
B	THR145
B	GLY146
B	ASP179
B	GLU183
B	ASN206
B	TYR224
B	ASN228

---

site_id	AC4
Number of Residues	12
Details	binding site for residue ZPN B 502

Chain	Residue
B	LEU217
B	HIS229
B	LEU230
B	ALA233
B	PHE272
B	PRO274
B	LEU275
B	THR276
B	GLN281
B	ARG284
B	GLN294
B	ARG369

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Functional Information from PROSITE/UniProt

site_id	PS00227
Number of Residues	7
Details	TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG

Chain	Residue	Details
B	GLY142-GLY148
A	GLY142-GLY148

---

site_id	PS00228
Number of Residues	4
Details	TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI

Chain	Residue	Details
B	MET1-ILE4

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	GLU254
B	SER140
B	GLY144
B	THR145
B	GLY146
B	ASN206
B	ASN228

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	GLN11
A	GLU71
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
A	ASN228

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	LYS40

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	SER48
A	SER232

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P68373

Chain	Residue	Details
A	TYR282

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	ARG339
B	THR292

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	LYS326
A	LYS370

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site_id	SWS_FT_FI8
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437

Chain	Residue	Details
B	LYS60

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site_id	SWS_FT_FI9
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437

Chain	Residue	Details
B	LYS326

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