Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WTV

Aurora-A Inhibitor Structure

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000212	biological_process	meiotic spindle organization
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000278	biological_process	mitotic cell cycle
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007052	biological_process	mitotic spindle organization
A	0007098	biological_process	centrosome cycle
A	0007100	biological_process	mitotic centrosome separation
A	0051321	biological_process	meiotic cell cycle
B	0000212	biological_process	meiotic spindle organization
B	0000226	biological_process	microtubule cytoskeleton organization
B	0000278	biological_process	mitotic cell cycle
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007052	biological_process	mitotic spindle organization
B	0007098	biological_process	centrosome cycle
B	0007100	biological_process	mitotic centrosome separation
B	0051321	biological_process	meiotic cell cycle
C	0000212	biological_process	meiotic spindle organization
C	0000226	biological_process	microtubule cytoskeleton organization
C	0000278	biological_process	mitotic cell cycle
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0007052	biological_process	mitotic spindle organization
C	0007098	biological_process	centrosome cycle
C	0007100	biological_process	mitotic centrosome separation
C	0051321	biological_process	meiotic cell cycle
D	0000212	biological_process	meiotic spindle organization
D	0000226	biological_process	microtubule cytoskeleton organization
D	0000278	biological_process	mitotic cell cycle
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0007052	biological_process	mitotic spindle organization
D	0007098	biological_process	centrosome cycle
D	0007100	biological_process	mitotic centrosome separation
D	0051321	biological_process	meiotic cell cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ZZL A 1390

Chain	Residue
A	GLY140
A	ALA273
A	ASP274
A	VAL279
A	ACT1392
A	HOH2015
A	HOH2072
A	HOH2111
A	HOH2163
C	LYS171
A	VAL147
A	LYS162
A	LEU194
A	GLU211
A	TYR212
A	ALA213
A	ASN261
A	LEU263

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1391

Chain	Residue
A	GLN231
A	ALA385
A	ASN386
A	SER387

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 1392

Chain	Residue
A	GLU217
A	GLU260
A	VAL279
A	ZZL1390
A	HOH2164

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT A 1393

Chain	Residue
A	HIS248
A	MET373
A	LEU374
A	HOH2165

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS A 1394

Chain	Residue
A	TYR148
A	ARG205
C	PRO138

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 1390

Chain	Residue
A	ASN146
A	TYR148
C	GLY136
C	ARG137
C	HOH2190
C	HOH2191

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ZZL B 1390

Chain	Residue
B	LEU139
B	LYS141
B	VAL147
B	LYS162
B	LEU194
B	GLU211
B	TYR212
B	ALA213
B	ASN261
B	LEU263
B	ALA273
B	ASP274
B	PHE275
B	ACT1393
B	HOH2101

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS B 1391

Chain	Residue
B	PRO138
D	TYR148
D	ARG205

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 1392

Chain	Residue
B	ASP256
B	LYS258
B	GLY291
B	THR292
B	HOH2192

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 1393

Chain	Residue
B	GLU217
B	LYS220
B	VAL279
B	ZZL1390
B	HOH2193

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 1394

Chain	Residue
B	EDO1399
B	HOH2194
B	HOH2195
D	ASN146

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 1395

Chain	Residue
B	GLU170
B	GLY173
B	GLU175
B	HIS176

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 1396

Chain	Residue
B	HIS201

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 1397

Chain	Residue
B	ASP202
B	ALA203
B	THR204

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 1398

Chain	Residue
B	HIS280
B	ALA281
B	TPO287
D	SER266
D	GLU269
D	HOH2131

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 1399

Chain	Residue
B	GLY136
B	ARG137
B	EDO1394
D	ASN146
D	TYR148

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 1391

Chain	Residue
B	ASP229
B	GLN231
B	HOH2074
C	ASP229
C	GLN231
C	ARG232
C	HOH2193
C	HOH2194

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT B 1400

Chain	Residue
B	HIS248
B	LYS309
B	MET373
B	LEU374
B	HOH2196
B	HOH2197

site_id	CC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ZZL C 1392

Chain	Residue
C	LEU139
C	LYS141
C	VAL147
C	LYS162
C	LEU194
C	GLU211
C	TYR212
C	ALA213
C	ASN261
C	LEU263
C	ALA273
C	ASP274
C	PHE275
C	VAL279
C	ACT1394
C	HOH2100

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT C 1393

Chain	Residue
C	HIS248
C	LYS309
C	MET373
C	LEU374
C	HOH2196

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT C 1394

Chain	Residue
C	GLU217
C	LYS220
C	ZZL1392
C	HOH2064

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 1395

Chain	Residue
C	ASP256
C	LYS258
C	GLY291
C	THR292
C	HOH2197

site_id	CC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ZZL D 1390

Chain	Residue
B	LYS171
D	GLY140
D	VAL147
D	LYS162
D	LEU194
D	GLU211
D	TYR212
D	ALA213
D	ASN261
D	LEU263
D	ALA273
D	ASP274
D	VAL279
D	ACT1392
D	HOH2017
D	HOH2132
D	HOH2179

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 1391

Chain	Residue
D	PHE346
D	PHE348
D	HOH2180
D	HOH2181

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT D 1392

Chain	Residue
D	GLU217
D	GLU260
D	VAL279
D	ZZL1390
D	HOH2182

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT D 1393

Chain	Residue
D	HIS248
D	LYS309
D	LEU374
D	HOH2183
D	HOH2184

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK

Chain	Residue	Details
A	LEU139-LYS162

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL

Chain	Residue	Details
A	VAL252-LEU264

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27837025","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G1X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19668197","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"11039908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"13678582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14580337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18662907","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19668197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26246606","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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