3W2C

Structure of Aurora kinase A complexed to benzoimidazole-indazole inhibitor XV

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
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
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
G	0000212	biological_process	meiotic spindle organization
G	0000226	biological_process	microtubule cytoskeleton organization
G	0000278	biological_process	mitotic cell cycle
G	0004672	molecular_function	protein kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
G	0007052	biological_process	mitotic spindle organization
G	0007098	biological_process	centrosome cycle
G	0007100	biological_process	mitotic centrosome separation
G	0051321	biological_process	meiotic cell cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE N15 A 401

Chain	Residue
A	ARG137
A	TYR212
A	ALA213
A	GLY216
A	LEU263
A	ALA273
A	ASP274
A	HOH509
A	LEU139
A	PHE144
A	VAL147
A	LYS162
A	GLN185
A	LEU194
A	LEU210
A	GLU211

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE N15 C 401

Chain	Residue
C	LEU139
C	LYS162
C	VAL182
C	GLN185
C	LEU194
C	LEU210
C	GLU211
C	TYR212
C	ALA213
C	GLY216
C	LEU263
C	ALA273
C	ASP274
C	HOH532

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE N15 E 401

Chain	Residue
E	LEU139
E	LYS162
E	GLN185
E	LEU194
E	LEU208
E	GLU211
E	TYR212
E	ALA213
E	GLY216
E	LEU263
E	ASP274
E	HOH515

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE N15 G 401

Chain	Residue
G	LEU139
G	PHE144
G	LYS162
G	GLN185
G	LEU194
G	LEU210
G	GLU211
G	TYR212
G	ALA213
G	GLY216
G	LEU263
G	ASP274

---

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	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337

Chain	Residue	Details
A	ASP256
C	ASP256
E	ASP256
G	ASP256

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X

Chain	Residue	Details
A	LYS143
C	ASP274
E	LYS143
E	LYS162
E	GLU211
E	GLU260
E	ASP274
G	LYS143
G	LYS162
G	GLU211
G	GLU260
A	LYS162
G	ASP274
A	GLU211
A	GLU260
A	ASP274
C	LYS143
C	LYS162
C	GLU211
C	GLU260

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197

Chain	Residue	Details
A	THR287
C	THR287
E	THR287
G	THR287

---

site_id	SWS_FT_FI4
Number of Residues	4
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
C	THR288
E	THR288
G	THR288

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726

Chain	Residue	Details
A	SER342
C	SER342
E	SER342
G	SER342

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS258
C	LYS258
E	LYS258
G	LYS258

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