5ZZ4

Crystal structure of bruton's tyrosine kinase in complex with inhibitor 2e

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
F	0004672	molecular_function	protein kinase activity
F	0004713	molecular_function	protein tyrosine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue 9M3 A 701

Chain	Residue
A	LEU408
A	ASN479
A	GLY480
A	ASP521
A	ASN526
A	LEU528
A	ASP539
A	LEU542
A	SER543
A	TYR551
A	GLY411
A	VAL416
A	ALA428
A	LYS430
A	GLU475
A	TYR476
A	MET477
A	ALA478

---

site_id	AC2
Number of Residues	19
Details	binding site for residue 9M3 B 701

Chain	Residue
B	LEU408
B	GLY411
B	GLN412
B	VAL416
B	ALA428
B	LYS430
B	THR474
B	GLU475
B	TYR476
B	MET477
B	ALA478
B	GLY480
B	ASP521
B	ASN526
B	LEU528
B	ASP539
B	LEU542
B	SER543
B	TYR551

---

site_id	AC3
Number of Residues	16
Details	binding site for residue 9M3 C 701

Chain	Residue
C	LEU408
C	VAL416
C	ALA428
C	LYS430
C	THR474
C	GLU475
C	TYR476
C	MET477
C	ALA478
C	GLY480
C	ASP521
C	ASN526
C	LEU528
C	ASP539
C	LEU542
C	TYR551

---

site_id	AC4
Number of Residues	18
Details	binding site for residue 9M3 D 701

Chain	Residue
D	LEU408
D	GLY411
D	GLN412
D	VAL416
D	ALA428
D	LYS430
D	THR474
D	GLU475
D	TYR476
D	MET477
D	ALA478
D	GLY480
D	ASP521
D	ASN526
D	LEU528
D	ASP539
D	SER543
D	TYR551

---

site_id	AC5
Number of Residues	16
Details	binding site for residue 9M3 E 701

Chain	Residue
E	LEU408
E	GLY411
E	GLN412
E	VAL416
E	ALA428
E	LYS430
E	THR474
E	GLU475
E	TYR476
E	MET477
E	ALA478
E	GLY480
E	ASN526
E	LEU528
E	ASP539
E	TYR551

---

site_id	AC6
Number of Residues	17
Details	binding site for residue 9M3 F 701

Chain	Residue
F	ASP521
F	ASN526
F	ASP539
F	SER543
F	TYR551
F	LEU408
F	GLY411
F	GLN412
F	VAL416
F	ALA428
F	LYS430
F	THR474
F	GLU475
F	TYR476
F	MET477
F	ALA478
F	GLY480

---

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	6
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
F	ASP521

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU408
E	LYS430
F	LEU408
F	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	6
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
F	THR474

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY

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

---

site_id	SWS_FT_FI5
Number of Residues	6
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
F	TYR551

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

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

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15375214

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

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15375214

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

---