6HJJ

Crystal structure of Aurora-A L210C catalytic domain in complex with ASDO6 ligand

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	14
Details	binding site for residue G7T A 501

Chain	Residue
A	LEU139
A	GLU211
A	ALA213
A	LEU263
A	ALA273
A	PHE275
A	GLY140
A	ALA160
A	LYS162
A	LEU169
A	VAL174
A	GLN177
A	LEU178
A	GLU181

---

site_id	AC2
Number of Residues	2
Details	binding site for residue CL A 502

Chain	Residue
A	THR333
A	GLU345

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site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 503

Chain	Residue
A	ARG343
A	HOH616

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site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 504

Chain	Residue
A	GLN335
A	HOH653

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site_id	AC5
Number of Residues	3
Details	binding site for residue ACT A 505

Chain	Residue
A	SER361
A	LYS365
A	HOH652

---

site_id	AC6
Number of Residues	3
Details	binding site for residue ACT A 506

Chain	Residue
A	ARG151
A	LYS156
A	ASN332

---

site_id	AC7
Number of Residues	6
Details	binding site for residue ACT A 507

Chain	Residue
A	ARG220
A	LYS224
A	HIS366
A	ASN367
A	HOH602
A	HOH639

---

site_id	AC8
Number of Residues	3
Details	binding site for residue PGF A 508

Chain	Residue
A	LEU225
A	SER226
A	LYS227

---

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

---

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

---

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

---

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	THR288

---

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

---

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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