7L5O

Crystal structure of the noncovalently bonded complex of rilzabrutinib with BTK

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	17
Details	binding site for residue R1L A 701

Chain	Residue
A	LEU408
A	ASN484
A	LEU528
A	SER538
A	ASP539
A	PHE540
A	HOH903
A	HOH956
A	HOH962
A	VAL416
A	ALA428
A	MET449
A	THR474
A	GLU475
A	MET477
A	GLY480
A	CYS481

---

site_id	AC2
Number of Residues	6
Details	binding site for residue DMS A 702

Chain	Residue
A	THR403
A	PHE404
A	TYR627
A	THR628
A	TYR631
A	HOH973

---

site_id	AC3
Number of Residues	4
Details	binding site for residue PEG A 703

Chain	Residue
A	TRP421
A	TYR461
A	HOH815
A	HOH1062

---

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 704

Chain	Residue
A	TYR598
A	GLU599
A	ARG600
A	HOH838
A	HOH844
A	HOH916

---

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 A 705

Chain	Residue
A	GLY389
A	ARG422

---

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

Chain	Residue
A	ALA478
A	ASN479
A	GLY480
A	HOH948
A	HOH956

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO A 707

Chain	Residue
A	ASP521
A	ASP539
A	SER543
A	HOH819
A	HOH843
A	HOH885

---

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	ASP521

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU408
A	LYS430

---

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	THR474

---

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

Chain	Residue	Details
A	LEU542

---

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	TYR551

---

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

Chain	Residue	Details
A	SER604

---

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

Chain	Residue	Details
A	TYR617

---

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

Chain	Residue	Details
A	SER623

---

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

Chain	Residue	Details
A	SER659

---