6S1J

Crystal Structure of DYRK1A with small molecule inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0046777	biological_process	protein autophosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue KRK A 501

Chain	Residue
A	ILE165
A	LEU294
A	VAL306
A	HOH677
A	GLY166
A	PHE170
A	VAL173
A	ALA186
A	LYS188
A	PHE238
A	GLU239
A	LEU241

---

site_id	AC2
Number of Residues	11
Details	binding site for residue EDO A 502

Chain	Residue
A	ASN198
A	GLN199
A	GLN199
A	ILE202
A	ILE202
A	TYR319
A	TYR319
A	HOH610
A	HOH610
A	HOH639
A	HOH639

---

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 503

Chain	Residue
A	THR466
A	ARG467
A	ILE468
A	GLN469
A	TYR472
A	HOH778

---

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

Chain	Residue
A	ALA382
A	HIS383

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 505

Chain	Residue
A	VAL376
A	LYS422
A	LEU423
A	HIS424

---

site_id	AC6
Number of Residues	5
Details	binding site for residue DMS A 506

Chain	Residue
A	ASN365
A	GLU366
A	VAL367
A	LYS393
A	SO4511

---

site_id	AC7
Number of Residues	5
Details	binding site for residue EDO A 507

Chain	Residue
A	MET336
A	ASP463
A	PRO464
A	LYS465
A	HOH603

---

site_id	AC8
Number of Residues	6
Details	binding site for residue EDO A 508

Chain	Residue
A	TYR243
A	ASN251
A	LEU274
A	HOH625
A	HOH652
A	HOH774

---

site_id	AC9
Number of Residues	7
Details	binding site for residue SO4 A 509

Chain	Residue
A	SER169
A	LYS193
A	LYS194
A	HOH613
A	HOH675
A	HOH701
A	HOH745

---

site_id	AD1
Number of Residues	6
Details	binding site for residue SO4 A 510

Chain	Residue
A	ASN144
A	TYR145
A	SER169
A	LYS191
A	LYS193
A	HOH641

---

site_id	AD2
Number of Residues	5
Details	binding site for residue SO4 A 511

Chain	Residue
A	ASN232
A	ARG325
A	ARG328
A	GLU366
A	DMS506

---

site_id	AD3
Number of Residues	4
Details	binding site for residue SO4 A 512

Chain	Residue
A	LYS264
A	ARG300
A	SER301
A	HOH805

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydrveqew..........VAIK

Chain	Residue	Details
A	ILE165-LYS188

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL

Chain	Residue	Details
A	ILE283-LEU295

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168

Chain	Residue	Details
A	ASP287

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	ILE165
A	LYS188
A	PHE238

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
A	TYR140
A	TYR159
A	TYR177
A	TYR319
A	PTR321
A	TYR449

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	TYR145

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470

Chain	Residue	Details
A	TYR219

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
A	SER310

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
A	THR402

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