6TVN

Crystal Structure of 5-bromoindoline-2,3-dione covalently bound to the PH domain of Bruton's tyrosine kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0035556	biological_process	intracellular signal transduction
B	0035556	biological_process	intracellular signal transduction
C	0035556	biological_process	intracellular signal transduction
D	0035556	biological_process	intracellular signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue NYQ A 201

Chain	Residue
A	LYS12
A	SER14
A	GLN15
A	LEU37
A	TYR39
A	ILE56

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 202

Chain	Residue
A	CYS165
A	HIS143
A	CYS154
A	CYS155

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 203

Chain	Residue
A	GLU96
B	HOH301
B	HOH302
B	HOH303
B	HOH312

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 202

Chain	Residue
B	HIS143
B	CYS154
B	CYS155
B	CYS165

---

site_id	AC5
Number of Residues	7
Details	binding site for residue NYQ C 201

Chain	Residue
C	LYS12
C	SER14
C	GLN15
C	LEU37
C	TYR39
C	ILE56
C	LEU111

---

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN C 202

Chain	Residue
C	HIS143
C	CYS154
C	CYS155
C	CYS165

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN D 202

Chain	Residue
D	HIS143
D	CYS154
D	CYS155
D	CYS165

---

site_id	AC8
Number of Residues	4
Details	binding site for residue MG D 203

Chain	Residue
C	HOH304
C	HOH305
D	GLU96
D	HOH301

---

site_id	AC9
Number of Residues	11
Details	binding site for Di-peptide NYQ B 201 and LYS B 12

Chain	Residue
B	LEU11
B	ARG13
B	SER14
B	GLN15
B	PHE25
B	LYS26
B	LEU37
B	TYR39
B	ILE56
B	LEU111
B	TYR112

---

site_id	AD1
Number of Residues	9
Details	binding site for Di-peptide NYQ D 201 and LYS D 12

Chain	Residue
D	LEU11
D	ARG13
D	SER14
D	GLN15
D	PHE25
D	LYS26
D	TYR39
D	LEU111
D	TYR112

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:10196129

Chain	Residue	Details
A	LYS26
C	ARG28
C	TYR39
C	LYS53
D	LYS26
D	ARG28
D	TYR39
D	LYS53
A	ARG28
A	TYR39
A	LYS53
B	LYS26
B	ARG28
B	TYR39
B	LYS53
C	LYS26

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00432, ECO:0000269|PubMed:10196129, ECO:0000269|PubMed:9218782, ECO:0000269|Ref.48

Chain	Residue	Details
A	HIS143
C	CYS154
C	CYS155
C	CYS165
D	HIS143
D	CYS154
D	CYS155
D	CYS165
A	CYS154
A	CYS155
A	CYS165
B	HIS143
B	CYS154
B	CYS155
B	CYS165
C	HIS143

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0000269|Ref.11, ECO:0007744|PubMed:25944712

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:16644721

Chain	Residue	Details
A	SER21
A	SER115
B	SER21
B	SER115
C	SER21
C	SER115
D	SER21
D	SER115

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P35991

Chain	Residue	Details
A	TYR40
B	TYR40
C	TYR40
D	TYR40

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER55
B	SER55
C	SER55
D	SER55

---