6TFP

BTK in complex with LOU064, a potent and highly selective covalent inhibitor

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
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
E	0004672	molecular_function	protein kinase activity
E	0004713	molecular_function	protein tyrosine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue NA A 701

Chain	Residue
A	HIS620
A	HOH878
A	HOH895
A	HOH937
A	HOH978
D	HOH880

---

site_id	AC2
Number of Residues	25
Details	binding site for residue N6Z A 702

Chain	Residue
A	GLN412
A	PHE413
A	VAL416
A	ALA428
A	LYS430
A	GLU475
A	MET477
A	CYS481
A	ASP521
A	ASN526
A	LEU528
A	SER538
A	ASP539
A	LEU542
A	SER543
A	VAL546
A	TYR551
A	HOH801
A	HOH820
A	HOH845
A	HOH887
A	HOH951
A	LEU408
A	GLY409
A	THR410

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA C 701

Chain	Residue
B	HOH812
C	HIS620
C	HOH830
C	HOH833
C	HOH852
C	HOH876

---

site_id	AC4
Number of Residues	32
Details	binding site for Di-peptide N6Z B 701 and CYS B 481

Chain	Residue
B	LEU408
B	GLY409
B	THR410
B	GLN412
B	PHE413
B	VAL416
B	ALA428
B	LYS430
B	GLU475
B	MET477
B	GLY480
B	LEU482
B	LEU483
B	ASN484
B	TYR485
B	ASP521
B	ARG525
B	ASN526
B	CYS527
B	LEU528
B	SER538
B	ASP539
B	LEU542
B	SER543
B	VAL546
B	TYR551
B	HOH803
B	HOH813
B	HOH842
B	HOH861
B	HOH862
B	HOH907

---

site_id	AC5
Number of Residues	29
Details	binding site for Di-peptide N6Z C 702 and CYS C 481

Chain	Residue
C	LEU408
C	GLY409
C	THR410
C	GLN412
C	PHE413
C	VAL416
C	ALA428
C	LYS430
C	GLU475
C	MET477
C	GLY480
C	LEU482
C	LEU483
C	ASN484
C	TYR485
C	ARG525
C	ASN526
C	CYS527
C	LEU528
C	SER538
C	ASP539
C	LEU542
C	SER543
C	VAL546
C	TYR551
C	HOH801
C	HOH814
C	HOH846
C	HOH853

---

site_id	AC6
Number of Residues	31
Details	binding site for Di-peptide N6Z D 701 and CYS D 481

Chain	Residue
D	GLY409
D	THR410
D	GLN412
D	PHE413
D	VAL416
D	ALA428
D	LYS430
D	GLU475
D	MET477
D	GLY480
D	LEU482
D	LEU483
D	ASN484
D	TYR485
D	ASP521
D	ARG525
D	ASN526
D	CYS527
D	LEU528
D	SER538
D	ASP539
D	LEU542
D	SER543
D	VAL546
D	TYR551
D	HOH813
D	HOH830
D	HOH834
D	HOH852
D	HOH887
D	LEU408

---

site_id	AC7
Number of Residues	31
Details	binding site for Di-peptide N6Z E 701 and CYS E 481

Chain	Residue
E	LEU408
E	GLY409
E	THR410
E	GLN412
E	PHE413
E	VAL416
E	ALA428
E	LYS430
E	GLU475
E	MET477
E	GLY480
E	LEU482
E	LEU483
E	ASN484
E	TYR485
E	ASP521
E	ARG525
E	ASN526
E	CYS527
E	LEU528
E	SER538
E	ASP539
E	LEU542
E	SER543
E	VAL546
E	TYR551
E	HOH802
E	HOH813
E	HOH814
E	HOH825
E	HOH842

---

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	5
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP521
B	ASP521
C	ASP521
D	ASP521
E	ASP521

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU408
E	LYS430
A	LYS430
B	LEU408
B	LYS430
C	LEU408
C	LYS430
D	LEU408
D	LYS430
E	LEU408

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:20052711, ECO:0007744|PDB:3K54, ECO:0007744|PDB:3OCT

Chain	Residue	Details
A	THR474
B	THR474
C	THR474
D	THR474
E	THR474

---

site_id	SWS_FT_FI4
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY

Chain	Residue	Details
A	LEU542
B	LEU542
C	LEU542
D	LEU542
E	LEU542

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	MOD_RES: Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8630736, ECO:0000269|PubMed:9012831

Chain	Residue	Details
A	TYR551
B	TYR551
C	TYR551
D	TYR551
E	TYR551

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER604
B	SER604
C	SER604
D	SER604
E	SER604

---

site_id	SWS_FT_FI7
Number of Residues	5
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15375214

Chain	Residue	Details
A	TYR617
B	TYR617
C	TYR617
D	TYR617
E	TYR617

---

site_id	SWS_FT_FI8
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15375214

Chain	Residue	Details
A	SER623
B	SER623
C	SER623
D	SER623
E	SER623

---

site_id	SWS_FT_FI9
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER659
B	SER659
C	SER659
D	SER659
E	SER659

---