5G1X

Crystal structure of Aurora-A kinase in complex with N-Myc

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	0003700	molecular_function	DNA-binding transcription factor activity
B	0006355	biological_process	regulation of DNA-templated transcription

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP A 1390

Chain	Residue
A	GLY140
A	ALA213
A	THR217
A	GLU260
A	ASN261
A	LEU263
A	ASP274
A	MG1391
A	MG1392
A	HOH2012
A	HOH2017
A	LYS141
A	HOH2026
A	HOH2111
A	HOH2112
A	HOH2114
A	HOH2184
A	HOH2188
A	HOH2189
A	GLY142
A	LYS143
A	VAL147
A	ALA160
A	LYS162
A	LEU194
A	GLU211

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 1391

Chain	Residue
A	ASP274
A	ADP1390
A	HOH2026
A	HOH2036
A	HOH2116
A	HOH2117
A	HOH2185

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

Chain	Residue
A	ASN261
A	ASP274
A	ADP1390
A	HOH2112
A	HOH2114

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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	LYS162
A	GLU211
A	GLU260
A	ASP274
A	LYS143

---

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

---

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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