6TUH

The PH domain of Bruton's tyrosine kinase mutant R28C

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 NXT A 201

Chain	Residue
A	LYS12
A	GLN15
A	ARG28
A	TYR39
A	LYS53
A	NXT202

---

site_id	AC2
Number of Residues	6
Details	binding site for residue NXT A 202

Chain	Residue
A	GLN16
A	LYS26
A	NXT201
A	LYS12
A	SER14
A	GLN15

---

site_id	AC3
Number of Residues	3
Details	binding site for residue MG A 203

Chain	Residue
A	GLU96
A	HOH313
B	GLY47

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN A 204

Chain	Residue
A	HIS143
A	CYS154
A	CYS155
A	CYS165

---

site_id	AC5
Number of Residues	4
Details	binding site for residue NXT B 201

Chain	Residue
B	LYS12
B	ARG28
B	TYR39
B	LYS53

---

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

Chain	Residue
B	HIS143
B	CYS154
B	CYS155
B	CYS165

---

site_id	AC7
Number of Residues	5
Details	binding site for residue ZN C 202

Chain	Residue
C	HIS143
C	TYR152
C	CYS154
C	CYS155
C	CYS165

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN D 202

Chain	Residue
D	HIS143
D	CYS154
D	CYS155
D	CYS165

---

site_id	AC9
Number of Residues	7
Details	binding site for Di-peptide NXT C 201 and LYS C 12

Chain	Residue
C	LEU11
C	ARG13
C	PHE25
C	LYS26
C	ARG28
C	TYR39
C	LYS53

---

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

Chain	Residue
D	LEU11
D	ARG13
D	SER14
D	PHE25
D	LYS26
D	ARG28
D	TYR39
D	LYS53
D	LEU111

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	144
Details	ZN_FING: Btk-type => ECO:0000255|PROSITE-ProRule:PRU00432

Chain	Residue	Details
A	PRO101-ASP137
B	PRO101-ASP137
C	PRO101-ASP137
D	PRO101-ASP137

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:10196129

Chain	Residue	Details
A	ILE5
A	LYS19
B	ILE5
B	LYS19
C	ILE5
C	LYS19
D	ILE5
D	LYS19

---

site_id	SWS_FT_FI3
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	GLY109
C	LEU120
C	ARG121
C	VAL131
D	GLY109
D	LEU120
D	ARG121
D	VAL131
A	LEU120
A	ARG121
A	VAL131
B	GLY109
B	LEU120
B	ARG121
B	VAL131
C	GLY109

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P35991

Chain	Residue	Details
A	LEU6
B	LEU6
C	LEU6
D	LEU6

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER21
B	SER21
C	SER21
D	SER21

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:16644721

Chain	Residue	Details
A	ARG81
B	ARG81
C	ARG81
D	ARG81

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKC/PRKCB => ECO:0000269|PubMed:11598012

Chain	Residue	Details
A	PHE146
B	PHE146
C	PHE146
D	PHE146

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	GLN157
B	GLN157
C	GLN157
D	GLN157

---