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	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027, ECO:0000269\|PubMed:14580337

Chain	Residue	Details
A	ASP256
B	ASP256
C	ASP256
D	ASP256
E	ASP256
F	ASP256

site_id	SWS_FT_FI2
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:27837025, ECO:0007744\|PDB:5G1X

Chain	Residue	Details
A	LYS143
B	ASP274
C	LYS143
C	LYS162
C	GLU211
C	GLU260
C	ASP274
D	LYS143
D	LYS162
D	GLU211
D	GLU260
A	LYS162
D	ASP274
E	LYS143
E	LYS162
E	GLU211
E	GLU260
E	ASP274
F	LYS143
F	LYS162
F	GLU211
F	GLU260
A	GLU211
F	ASP274
A	GLU260
A	ASP274
B	LYS143
B	LYS162
B	GLU211
B	GLU260

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:14580337, ECO:0000269\|PubMed:19668197

Chain	Residue	Details
A	ASP287
B	ASP287
C	ASP287
D	ASP287
E	ASP287
F	ASP287

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:11039908, ECO:0000269\|PubMed:13678582, ECO:0000269\|PubMed:14580337, ECO:0000269\|PubMed:16246726, ECO:0000269\|PubMed:18662907, ECO:0000269\|PubMed:19668197, ECO:0000269\|PubMed:26246606

Chain	Residue	Details
A	ASP288
B	ASP288
C	ASP288
D	ASP288
E	ASP288
F	ASP288

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269\|PubMed:16246726

Chain	Residue	Details
A	SER342
B	SER342
C	SER342
D	SER342
E	SER342
F	SER342

site_id	SWS_FT_FI6
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS258
F	LYS258
B	LYS258
C	LYS258
D	LYS258
E	LYS258

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