Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5FNV

a new complex structure of tubulin with an alpha-beta unsaturated lactone

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0030182	biological_process	neuron differentiation
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000226	biological_process	microtubule cytoskeleton organization
B	0000278	biological_process	mitotic cell cycle
B	0001764	biological_process	neuron migration
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
C	0000166	molecular_function	nucleotide binding
C	0000226	biological_process	microtubule cytoskeleton organization
C	0000278	biological_process	mitotic cell cycle
C	0003924	molecular_function	GTPase activity
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005874	cellular_component	microtubule
C	0007017	biological_process	microtubule-based process
C	0015630	cellular_component	microtubule cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0030182	biological_process	neuron differentiation
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0000226	biological_process	microtubule cytoskeleton organization
D	0000278	biological_process	mitotic cell cycle
D	0001764	biological_process	neuron migration
D	0003924	molecular_function	GTPase activity
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005515	molecular_function	protein binding
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005874	cellular_component	microtubule
D	0007017	biological_process	microtubule-based process
D	0046872	molecular_function	metal ion binding
E	0031110	biological_process	regulation of microtubule polymerization or depolymerization
F	0036211	biological_process	protein modification process

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE GTP A 1438

Chain	Residue
A	GLY10
A	GLY144
A	THR145
A	GLY146
A	VAL177
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	ILE231
A	MG1439
A	GLN11
A	HOH2001
A	HOH2002
A	HOH2004
A	HOH2005
A	HOH2006
A	HOH2007
A	HOH2009
B	LYS252
A	ALA12
A	GLN15
A	ASP98
A	ALA99
A	ASN101
A	SER140
A	GLY143

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1439

Chain	Residue
A	GTP1438
A	HOH2002
A	HOH2004
A	HOH2005
A	HOH2006

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 1440

Chain	Residue
A	ASP39
A	THR41
A	GLY44
A	GLU55

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GDP B 1429

Chain	Residue
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	SER138
B	GLY141
B	GLY142
B	THR143
B	GLY144
B	PRO171
B	VAL175
B	ASP177
B	GLU181
B	ASN204
B	TYR222
B	ASN226
B	MG1430
B	HOH2001
B	HOH2002
B	HOH2003
B	HOH2004
B	HOH2007
B	HOH2008

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 1430

Chain	Residue
B	GLN11
B	ASP177
B	GDP1429
B	HOH2002

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA B 1431

Chain	Residue
B	GLU111
C	TYR282

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MES B 1432

Chain	Residue
B	ARG156
B	PRO160
B	ASP161
B	ARG162
B	ASN195
B	ASP197
B	ARG251

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MES B 1433

Chain	Residue
B	PHE294
B	ASP295
B	ALA296
B	ASP304
B	ARG306
B	ASN337
B	TYR340
B	HOH2013

site_id	AC9
Number of Residues	28
Details	BINDING SITE FOR RESIDUE GTP C 1440

Chain	Residue
C	MG1441
C	HOH2002
C	HOH2003
C	HOH2005
C	HOH2006
C	HOH2008
C	HOH2015
C	HOH2020
D	LYS252
C	GLY10
C	GLN11
C	ALA12
C	GLN15
C	ASP98
C	ALA99
C	ALA100
C	ASN101
C	SER140
C	GLY143
C	GLY144
C	THR145
C	GLY146
C	VAL177
C	GLU183
C	ASN206
C	TYR224
C	ASN228
C	ILE231

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1441

Chain	Residue
C	GTP1440
C	HOH2003
C	HOH2005
C	HOH2006
C	HOH2008

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 1442

Chain	Residue
C	ASP39
C	THR41
C	GLY44
C	GLU55

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ACP F 1385

Chain	Residue
F	LYS74
F	ILE148
F	LYS150
F	GLN183
F	LYS184
F	TYR185
F	LEU186
F	LYS198
F	ASP200
F	ARG202
F	ARG222
F	HIS239
F	THR241
F	ASN242
F	ASP318
F	ILE330
F	GLU331
F	ASN333

site_id	BC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GTP D 1431

Chain	Residue
D	GLY10
D	GLN11
D	CYS12
D	GLN15
D	ALA97
D	GLY98
D	ASN99
D	SER138
D	GLY141
D	GLY142
D	THR143
D	GLY144
D	SER176
D	GLU181
D	ASN204
D	TYR222
D	ASN226
D	MG1432

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 1432

Chain	Residue
D	GLU69
D	GTP1431

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
A	GLY142-GLY148
B	GLY140-GLY146

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

Chain	Residue	Details
B	MET1-ILE4

site_id	PS00563
Number of Residues	10
Details	STATHMIN_1 Stathmin family signature 1. PRRRDpSLEE

Chain	Residue	Details
E	PRO40-GLU49

site_id	PS01041
Number of Residues	10
Details	STATHMIN_2 Stathmin family signature 2. AEKREHEREV

Chain	Residue	Details
E	ALA73-VAL82

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Motif: {"description":"MREC motif","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	35
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q13885","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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