5OS1

Crystal structure of Aurora-A kinase in complex with an allosterically binding fragment

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	binding site for residue ADP A 401

Chain	Residue
A	GLY140
A	GLU211
A	ALA213
A	THR217
A	GLU260
A	ASN261
A	LEU263
A	ASP274
A	MG402
A	MG403
A	HOH507
A	GLY142
A	HOH519
A	HOH555
A	HOH563
A	HOH566
A	HOH567
A	HOH575
A	HOH578
A	LYS143
A	PHE144
A	GLY145
A	VAL147
A	ALA160
A	LYS162
A	LEU194

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 402

Chain	Residue
A	ASN261
A	ASP274
A	ADP401
A	HOH555
A	HOH567

---

site_id	AC3
Number of Residues	6
Details	binding site for residue MG A 403

Chain	Residue
A	ASP274
A	ADP401
A	HOH507
A	HOH566
A	HOH588
A	HOH590

---

site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 404

Chain	Residue
A	SER284
A	SER284

---

site_id	AC5
Number of Residues	4
Details	binding site for residue CL A 405

Chain	Residue
A	ARG255
A	ARG286
A	THR287
A	HOH529

---

site_id	AC6
Number of Residues	2
Details	binding site for residue CL A 406

Chain	Residue
A	LEU374
A	ARG375

---

site_id	AC7
Number of Residues	4
Details	binding site for residue A7H A 407

Chain	Residue
A	GLU170
A	GLU175
A	ARG179
A	TYR199

---

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	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	TPO288

---

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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