5L8J

Aurora-A kinase domain in complex with vNAR-D01 S93R

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	0019815	cellular_component	B cell receptor complex
B	0042101	cellular_component	T cell receptor complex
B	0042605	molecular_function	peptide antigen binding
B	0050853	biological_process	B cell receptor signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue ADP A 501

Chain	Residue
A	LEU139
A	HOH623
A	HOH689
A	HOH697
A	HOH704
A	GLY140
A	GLY142
A	LYS143
A	VAL147
A	ALA160
A	LYS162
A	GLU211
A	ALA213

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site_id	AC2
Number of Residues	6
Details	binding site for residue EDO A 502

Chain	Residue
A	TRP128
A	GLY198
A	TYR199
A	HOH626
A	HOH669
B	ARG93

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

Chain	Residue
A	THR235
A	SER388

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site_id	AC4
Number of Residues	4
Details	binding site for residue PEG A 504

Chain	Residue
A	LYS153
A	HOH604
B	MET1
B	ALA2

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site_id	AC5
Number of Residues	2
Details	binding site for residue PEG A 505

Chain	Residue
A	ASP358
A	PRO381

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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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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

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

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

---

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

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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

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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

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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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