6CPG

Structure of dephosphorylated Aurora A (122-403) in complex with inhibiting monobody and AT9283 in an inactive conformation

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
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	6
Details	binding site for residue 35R A 501

Chain	Residue
A	LEU139
A	VAL147
A	ALA160
A	GLU211
A	ALA213
A	GLY216

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site_id	AC2
Number of Residues	9
Details	binding site for residue 35R D 501

Chain	Residue
D	ALA213
D	PRO214
D	GLY216
D	ARG220
D	LEU263
D	THR347
D	LEU139
D	GLY140
D	GLU211

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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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site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP

Chain	Residue	Details
B	GLY39-PRO46

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337

Chain	Residue	Details
A	ASP256
D	ASP256

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site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X

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

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197

Chain	Residue	Details
A	THR287
D	THR287

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site_id	SWS_FT_FI4
Number of Residues	2
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	THR288
D	THR288

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726

Chain	Residue	Details
A	SER342
D	SER342

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site_id	SWS_FT_FI6
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS258
D	LYS258

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