6C83

Structure of Aurora A (122-403) bound to inhibitory Monobody Mb2 and AMPPCP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue ACP A 501

Chain	Residue
A	LEU139
A	GLY140
A	LYS141
A	GLY142
A	LYS143
A	ALA160
A	GLU211
A	ALA213

---

site_id	AC2
Number of Residues	9
Details	binding site for residue ACP B 501

Chain	Residue
B	GLY142
B	VAL147
B	ALA160
B	LEU194
B	GLU211
B	ALA213
B	THR217
B	LEU263
B	LEU139

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	GLY39-PRO46

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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	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
B	ASP256

---

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

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

---

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
B	THR287

---

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
B	THR288

---

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
B	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
B	LYS258
A	LYS258

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