5U9D

Discovery of a potent BTK inhibitor with a novel binding mode using parallel selections with a DNA-encoded chemical library

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine 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	20
Details	binding site for residue 83P A 701

Chain	Residue
A	LEU408
A	LYS430
A	MET431
A	ILE472
A	GLU475
A	MET477
A	LEU528
A	ASP539
A	HOH899
A	HOH908
A	HOH958
A	GLY409
A	HOH1033
A	THR410
A	GLY411
A	GLN412
A	PHE413
A	GLY414
A	VAL416
A	ALA428

---

site_id	AC2
Number of Residues	10
Details	binding site for residue EDO A 702

Chain	Residue
A	LYS400
A	TYR571
A	LYS573
A	ARG618
A	HIS620
A	LEU621
A	ALA622
A	SER623
A	HOH803
A	HOH876

---

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 703

Chain	Residue
A	TYR598
A	GLU599
A	ARG600
A	HOH830
A	HOH859
A	HOH870

---

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 704

Chain	Residue
A	PHE404
A	GLU407
A	LYS417

---

site_id	AC5
Number of Residues	2
Details	binding site for residue PEG A 705

Chain	Residue
A	TRP421
A	TYR461

---

site_id	AC6
Number of Residues	5
Details	binding site for residue PEG A 706

Chain	Residue
A	LYS420
A	GLN424
A	TYR425
A	ASP426
A	HOH894

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	23
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGQFGVVKyGkwrgqyd...........VAIK

Chain	Residue	Details
A	LEU408-LYS430

---

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV

Chain	Residue	Details
A	PHE517-VAL529

---

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:PRU10028

Chain	Residue	Details
A	ARG487

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	GLU396

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:20052711, ECO:0007744|PDB:3K54, ECO:0007744|PDB:3OCT

Chain	Residue	Details
A	ASP440

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY

Chain	Residue	Details
A	ALA508

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8630736, ECO:0000269|PubMed:9012831

Chain	Residue	Details
A	PHE517

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	MET570

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15375214

Chain	Residue	Details
A	PHE583

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15375214

Chain	Residue	Details
A	GLU589

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	LYS625

---