5BPY

Crystal structure of bruton agammaglobulinemia tyrosine kinase complexed with BMS-824171 AKA 6-[(3R)-3-(4-tert-bu tylbenzamido)piperidin-1-yl]-2-{[4-(morpholine-4-carbonyl) phenyl]amino}pyridine-3-carboxamide

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue 4UQ A 4000

Chain	Residue
A	LEU408
A	GLY480
A	CYS481
A	LEU528
A	VAL416
A	ALA428
A	THR474
A	GLU475
A	TYR476
A	MET477
A	ALA478
A	ASN479

---

site_id	AC2
Number of Residues	12
Details	binding site for residue 4UQ B 4000

Chain	Residue
B	VAL416
B	ALA428
B	THR474
B	GLU475
B	TYR476
B	MET477
B	ALA478
B	ASN479
B	GLY480
B	CYS481
B	ASN484
B	LEU528

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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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP521
B	ASP521

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU408
A	LYS430
B	LEU408
B	LYS430

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20052711, ECO:0007744|PDB:3K54, ECO:0007744|PDB:3OCT

Chain	Residue	Details
A	THR474
B	THR474

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY

Chain	Residue	Details
A	LEU542
B	LEU542

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8630736, ECO:0000269|PubMed:9012831

Chain	Residue	Details
A	TYR551
B	TYR551

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER604
B	SER604

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15375214

Chain	Residue	Details
A	TYR617
B	TYR617

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site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15375214

Chain	Residue	Details
A	SER623
B	SER623

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site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER659
B	SER659

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