8H65

Crystal structure of human GCN5 histone acetyltransferase domain bound with butyryl-CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004402	molecular_function	histone acetyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0004402	molecular_function	histone acetyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0004402	molecular_function	histone acetyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0004402	molecular_function	histone acetyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
E	0004402	molecular_function	histone acetyltransferase activity
E	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
F	0004402	molecular_function	histone acetyltransferase activity
F	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
G	0004402	molecular_function	histone acetyltransferase activity
G	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
H	0004402	molecular_function	histone acetyltransferase activity
H	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	153
Details	Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	72
Details	Region: {"description":"Loop 3","evidences":[{"source":"PubMed","id":"29211711","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	8
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"27796307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31527837","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29211711","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TRL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23142079","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
A	PHE568	electrostatic stabiliser
A	PHE573	electrostatic stabiliser
A	GLU575	proton acceptor
A	ILE576	electrostatic stabiliser
A	VAL577	electrostatic stabiliser
A	CYS579	electrostatic stabiliser
A	LEU611	electrostatic stabiliser
A	ILE642	electrostatic stabiliser
A	TYR645	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
B	PHE568	electrostatic stabiliser
B	PHE573	electrostatic stabiliser
B	GLU575	proton acceptor
B	ILE576	electrostatic stabiliser
B	VAL577	electrostatic stabiliser
B	CYS579	electrostatic stabiliser
B	LEU611	electrostatic stabiliser
B	ILE642	electrostatic stabiliser
B	TYR645	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
C	PHE568	electrostatic stabiliser
C	PHE573	electrostatic stabiliser
C	GLU575	proton acceptor
C	ILE576	electrostatic stabiliser
C	VAL577	electrostatic stabiliser
C	CYS579	electrostatic stabiliser
C	LEU611	electrostatic stabiliser
C	ILE642	electrostatic stabiliser
C	TYR645	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
D	PHE568	electrostatic stabiliser
D	PHE573	electrostatic stabiliser
D	GLU575	proton acceptor
D	ILE576	electrostatic stabiliser
D	VAL577	electrostatic stabiliser
D	CYS579	electrostatic stabiliser
D	LEU611	electrostatic stabiliser
D	ILE642	electrostatic stabiliser
D	TYR645	electrostatic stabiliser

---

site_id	MCSA5
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
E	PHE568	electrostatic stabiliser
E	PHE573	electrostatic stabiliser
E	GLU575	proton acceptor
E	ILE576	electrostatic stabiliser
E	VAL577	electrostatic stabiliser
E	CYS579	electrostatic stabiliser
E	LEU611	electrostatic stabiliser
E	ILE642	electrostatic stabiliser
E	TYR645	electrostatic stabiliser

---

site_id	MCSA6
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
F	PHE568	electrostatic stabiliser
F	PHE573	electrostatic stabiliser
F	GLU575	proton acceptor
F	ILE576	electrostatic stabiliser
F	VAL577	electrostatic stabiliser
F	CYS579	electrostatic stabiliser
F	LEU611	electrostatic stabiliser
F	ILE642	electrostatic stabiliser
F	TYR645	electrostatic stabiliser

---

site_id	MCSA7
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
G	PHE568	electrostatic stabiliser
G	PHE573	electrostatic stabiliser
G	GLU575	proton acceptor
G	ILE576	electrostatic stabiliser
G	VAL577	electrostatic stabiliser
G	CYS579	electrostatic stabiliser
G	LEU611	electrostatic stabiliser
G	ILE642	electrostatic stabiliser
G	TYR645	electrostatic stabiliser

---

site_id	MCSA8
Number of Residues	9
Details	M-CSA 524

Chain	Residue	Details
H	PHE568	electrostatic stabiliser
H	PHE573	electrostatic stabiliser
H	GLU575	proton acceptor
H	ILE576	electrostatic stabiliser
H	VAL577	electrostatic stabiliser
H	CYS579	electrostatic stabiliser
H	LEU611	electrostatic stabiliser
H	ILE642	electrostatic stabiliser
H	TYR645	electrostatic stabiliser

---