6NFH

BTK in complex with inhibitor 8-(2,3-dihydro-1H-inden-5-yl)-2-({4-[(2S)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}amino)-5,8-dihydropteridine-6,7-dione

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	13
Details	binding site for residue KLM A 701

Chain	Residue
A	LEU408
A	GLY480
A	LEU528
A	HOH807
A	HOH898
A	GLY409
A	THR410
A	VAL416
A	ALA428
A	LYS430
A	THR474
A	GLU475
A	MET477

---

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

Chain	Residue
A	HIS635
A	GLU636
A	HOH802
A	HOH804
A	HOH900
A	HOH933

---

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

Chain	Residue
A	TYR598
A	GLU599
A	ARG600
A	PHE601
A	HOH821
A	HOH833
A	HOH917

---

site_id	AC4
Number of Residues	7
Details	binding site for residue EDO A 704

Chain	Residue
A	TYR476
A	ALA478
A	ASN530
A	ASP531
A	HOH812
A	HOH966
A	HOH1035

---

site_id	AC5
Number of Residues	7
Details	binding site for residue EDO A 705

Chain	Residue
A	LYS400
A	LYS573
A	ARG618
A	HIS620
A	ALA622
A	SER623
A	HOH1076

---

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO A 706

Chain	Residue
A	ARG525
A	LYS558
A	PHE559
A	PRO560
A	TRP563
A	HOH868
A	HOH903

---

site_id	AC7
Number of Residues	5
Details	binding site for residue EDO A 707

Chain	Residue
A	VAL458
A	SER538
A	ASP539
A	PHE540
A	LEU542

---

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

---