6AUA

CRYSTAL STRUCTURE OF BRUTON'S TYROSINE KINASE IN COMPLEX WITH INHIBITOR CGI2625

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	8
Details	binding site for residue GOL A 701

Chain	Residue
A	ARG520
A	SER543
A	TYR551
A	PRO560
A	PHE574
A	HOH816
A	HOH821
A	HOH839

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site_id	AC2
Number of Residues	6
Details	binding site for residue SO4 A 702

Chain	Residue
A	ARG487
A	ARG490
A	LYS595
A	HOH826
A	HOH828
A	LYS466

---

site_id	AC3
Number of Residues	7
Details	binding site for residue SO4 A 703

Chain	Residue
A	SER592
A	LYS595
A	TYR617
A	PRO619
A	HIS620
A	HOH823
A	HOH899

---

site_id	AC4
Number of Residues	21
Details	binding site for residue BXJ A 704

Chain	Residue
A	LEU408
A	GLN412
A	VAL416
A	ALA428
A	LYS430
A	TYR476
A	MET477
A	ALA478
A	GLY480
A	ASP521
A	ASN526
A	LEU528
A	ASP539
A	LEU542
A	SER543
A	VAL546
A	TYR551
A	HOH843
A	HOH861
A	HOH897
A	HOH912

---

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

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