Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BMC

Aurora-2 T287D T288D complexed with PHA-680632

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
E	0000212	biological_process	meiotic spindle organization
E	0000226	biological_process	microtubule cytoskeleton organization
E	0000278	biological_process	mitotic cell cycle
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
E	0007052	biological_process	mitotic spindle organization
E	0007098	biological_process	centrosome cycle
E	0007100	biological_process	mitotic centrosome separation
E	0051321	biological_process	meiotic cell cycle
F	0000212	biological_process	meiotic spindle organization
F	0000226	biological_process	microtubule cytoskeleton organization
F	0000278	biological_process	mitotic cell cycle
F	0004672	molecular_function	protein kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
F	0007052	biological_process	mitotic spindle organization
F	0007098	biological_process	centrosome cycle
F	0007100	biological_process	mitotic centrosome separation
F	0051321	biological_process	meiotic cell cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MPY A1395

Chain	Residue
A	GLY140
A	PRO214
A	GLY216
A	GLU260
A	ASN261
A	LEU263
B	SER266
B	ALA267
B	GLY268
A	LYS141
A	GLY142
A	VAL147
A	ALA160
A	LYS162
A	GLU211
A	TYR212
A	ALA213

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MPY B1395

Chain	Residue
B	GLY140
B	LYS141
B	VAL147
B	ALA160
B	LYS162
B	GLU211
B	TYR212
B	ALA213
B	PRO214
B	GLY216
B	LYS224
B	GLU260
B	ASN261
B	LEU263

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE MPY C1394

Chain	Residue
C	GLY140
C	LYS141
C	GLY142
C	VAL147
C	ALA160
C	LYS162
C	LEU194
C	GLU211
C	TYR212
C	ALA213
C	PRO214
C	GLY216
C	GLU260
C	ASN261
C	LEU263

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE MPY D1395

Chain	Residue
C	LEU215
D	GLY140
D	LYS141
D	VAL147
D	ALA160
D	LYS162
D	GLU211
D	TYR212
D	ALA213
D	PRO214
D	GLY216
D	THR217
D	GLU260
D	ASN261
D	LEU263

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MPY E1395

Chain	Residue
E	GLY140
E	LYS141
E	GLY142
E	VAL147
E	ALA160
E	LYS162
E	GLU211
E	TYR212
E	ALA213
E	PRO214
E	GLY216
E	GLU260
E	ASN261
E	LEU263

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MPY F1395

Chain	Residue
E	SER266
F	LEU139
F	GLY140
F	VAL147
F	ALA160
F	LYS162
F	GLU211
F	TYR212
F	ALA213
F	PRO214
F	GLU260
F	ASN261
F	LEU263

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	6
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	36
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	6
Details	Modified residue: {"description":"Phosphoserine; by PKA and PAK","evidences":[{"source":"PubMed","id":"16246726","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP256
A	GLU260

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP256
B	GLU260

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP256
C	GLU260

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP256
D	GLU260

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP256
E	GLU260

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	ASP256
F	GLU260

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS258
A	ASP256

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	LYS258
B	ASP256

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	LYS258
C	ASP256

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	LYS258
D	ASP256

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	LYS258
E	ASP256

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	LYS258
F	ASP256

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	THR292
A	LYS258
A	ASP256

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	THR292
B	LYS258
B	ASP256

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	THR292
C	LYS258
C	ASP256

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	THR292
D	LYS258
D	ASP256

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	THR292
E	LYS258
E	ASP256

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	THR292
F	LYS258
F	ASP256

site_id	CSA19
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS258
A	ASN261
A	ASP256

site_id	CSA20
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	LYS258
B	ASN261
B	ASP256

site_id	CSA21
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	LYS258
C	ASN261
C	ASP256

site_id	CSA22
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	LYS258
D	ASN261
D	ASP256

site_id	CSA23
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	LYS258
E	ASN261
E	ASP256

site_id	CSA24
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
F	LYS258
F	ASN261
F	ASP256

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)