5DN3

Aurora A in complex with ATP and AA35.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 401

Chain	Residue
A	ASN261
A	ASP274
A	ATP404
A	HOH585
A	HOH607

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site_id	AC2
Number of Residues	5
Details	binding site for residue 5DN A 402

Chain	Residue
A	HIS201
A	LYS166
A	LEU169
A	GLU175
A	TYR199

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site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 403

Chain	Residue
A	ARG180
A	VAL279
A	HIS280
A	ARG285

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site_id	AC4
Number of Residues	29
Details	binding site for residue ATP A 404

Chain	Residue
A	GLY140
A	GLY142
A	LYS143
A	PHE144
A	GLY145
A	VAL147
A	ALA160
A	LYS162
A	GLU181
A	LEU194
A	GLU211
A	ALA213
A	THR217
A	GLU260
A	ASN261
A	LEU263
A	ASP274
A	GLY276
A	MG401
A	HOH507
A	HOH521
A	HOH531
A	HOH543
A	HOH552
A	HOH585
A	HOH591
A	HOH600
A	HOH604
A	HOH607

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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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337

Chain	Residue	Details
A	ASP256

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

Chain	Residue	Details
A	LYS143
A	LYS162
A	GLU211
A	GLU260
A	ASP274

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197

Chain	Residue	Details
A	THR287

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site_id	SWS_FT_FI4
Number of Residues	1
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	TPO288

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726

Chain	Residue	Details
A	SER342

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site_id	SWS_FT_FI6
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS258

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