4YLK

Crystal structure of DYRK1A in complex with 10-Chloro-substituted 11H-indolo[3,2-c]quinolone-6-carboxylic acid inhibitor 5s

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	9
Details	binding site for residue SO4 A 501

Chain	Residue
A	ARG325
A	ARG328
A	GLU366
A	SO4505
A	HOH603
A	HOH624
A	HOH669
A	HOH680
A	HOH1083

---

site_id	AC2
Number of Residues	8
Details	binding site for residue SO4 A 502

Chain	Residue
A	SER169
A	LYS193
A	LYS194
A	HOH648
A	HOH683
A	HOH692
A	HOH713
A	HOH906

---

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 A 503

Chain	Residue
A	LYS264
A	ARG300
A	SER301
A	HOH1015
A	HOH1122
A	HOH1124

---

site_id	AC4
Number of Residues	8
Details	binding site for residue SO4 A 504

Chain	Residue
A	ASN144
A	TYR145
A	SER169
A	LYS191
A	LYS193
A	HOH650
A	HOH682
A	HOH697

---

site_id	AC5
Number of Residues	8
Details	binding site for residue SO4 A 505

Chain	Residue
A	ASN365
A	GLU366
A	VAL367
A	LYS393
A	SO4501
A	HOH669
A	HOH721
A	HOH1025

---

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 A 506

Chain	Residue
A	LYS218
A	TYR219
A	ARG250
A	HOH640
A	HOH684

---

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

Chain	Residue
A	PRO279
A	GLU280
A	GLN313
A	GLY315
A	HOH1038

---

site_id	AC8
Number of Residues	4
Details	binding site for residue EDO A 508

Chain	Residue
A	ARG226
A	EDO509
A	HOH901
A	HOH1115

---

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO A 509

Chain	Residue
A	GLU183
A	HIS223
A	LYS225
A	ARG226
A	EDO508
A	HOH1040

---

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

Chain	Residue
A	LYS175
A	TYR472
A	EDO515
A	HOH605
A	HOH610
A	HOH638

---

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO A 511

Chain	Residue
A	LEU241
A	CYS296
A	ASN297
A	PRO298
A	HOH605
A	HOH630

---

site_id	AD3
Number of Residues	5
Details	binding site for residue EDO A 512

Chain	Residue
A	SER258
A	ASN260
A	HOH928
A	HOH1017
A	HOH1054

---

site_id	AD4
Number of Residues	11
Details	binding site for residue EDO A 513

Chain	Residue
A	ASN198
A	GLN199
A	GLN199
A	ILE202
A	ILE202
A	TYR319
A	TYR319
A	HOH602
A	HOH602
A	HOH632
A	HOH632

---

site_id	AD5
Number of Residues	7
Details	binding site for residue EDO A 514

Chain	Residue
A	PRO337
A	TYR338
A	ASP339
A	PRO464
A	LYS465
A	HOH783
A	HOH1067

---

site_id	AD6
Number of Residues	10
Details	binding site for residue EDO A 515

Chain	Residue
A	TYR472
A	EDO510
A	HOH604
A	HOH610
A	HOH638
A	LYS465
A	THR466
A	ARG467
A	ILE468
A	GLN469

---

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO A 516

Chain	Residue
A	PRO381
A	ALA382
A	HIS383
A	HOH1023

---

site_id	AD8
Number of Residues	2
Details	binding site for residue EDO A 517

Chain	Residue
A	TYR140
A	ARG231

---

site_id	AD9
Number of Residues	5
Details	binding site for residue EDO A 518

Chain	Residue
A	ASP454
A	LEU457
A	ARG458
A	HOH883
A	HOH965

---

site_id	AE1
Number of Residues	14
Details	binding site for residue 4E2 A 519

Chain	Residue
A	GLY166
A	LYS167
A	PHE170
A	ALA186
A	LYS188
A	PHE238
A	GLU239
A	LEU241
A	LEU294
A	ASP307
A	IOD520
A	HOH701
A	HOH808
A	HOH820

---

site_id	AE2
Number of Residues	6
Details	binding site for residue IOD A 520

Chain	Residue
A	GLY166
A	LYS167
A	GLN475
A	4E2519
A	HOH710
A	HOH775

---

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

---