6J6T

Crystal Structure of HDA15 HD domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000118	cellular_component	histone deacetylase complex
A	0004407	molecular_function	histone deacetylase activity
A	0006325	biological_process	chromatin organization
A	0016575	biological_process	histone deacetylation
B	0000118	cellular_component	histone deacetylase complex
B	0004407	molecular_function	histone deacetylase activity
B	0006325	biological_process	chromatin organization
B	0016575	biological_process	histone deacetylation
C	0000118	cellular_component	histone deacetylase complex
C	0004407	molecular_function	histone deacetylase activity
C	0006325	biological_process	chromatin organization
C	0016575	biological_process	histone deacetylation
D	0000118	cellular_component	histone deacetylase complex
D	0004407	molecular_function	histone deacetylase activity
D	0006325	biological_process	chromatin organization
D	0016575	biological_process	histone deacetylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue ZN A 601

Chain	Residue
A	ASP313
A	HIS315
A	ASP404

---

site_id	AC2
Number of Residues	5
Details	binding site for residue K A 602

Chain	Residue
A	ASP311
A	ASP313
A	HIS315
A	SER334
A	LEU335

---

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 A 603

Chain	Residue
A	LYS205
A	GLN206
C	THR213
C	SER214
C	GLU215
A	THR204

---

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 A 604

Chain	Residue
A	THR213
A	SER214
A	GLU215
A	HOH704

---

site_id	AC5
Number of Residues	3
Details	binding site for residue ZN B 601

Chain	Residue
B	ASP313
B	HIS315
B	ASP404

---

site_id	AC6
Number of Residues	5
Details	binding site for residue K B 602

Chain	Residue
B	ASP311
B	ASP313
B	HIS315
B	SER334
B	LEU335

---

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 B 603

Chain	Residue
B	ASN327
B	LYS328
B	SER329

---

site_id	AC8
Number of Residues	4
Details	binding site for residue SO4 B 604

Chain	Residue
B	ASN445
B	ARG447
D	SER148
D	LYS265

---

site_id	AC9
Number of Residues	7
Details	binding site for residue SO4 B 605

Chain	Residue
A	ARG157
A	ARG243
A	HOH770
B	THR204
B	LYS205
B	ARG246
B	HOH743

---

site_id	AD1
Number of Residues	3
Details	binding site for residue ZN C 601

Chain	Residue
C	ASP313
C	HIS315
C	ASP404

---

site_id	AD2
Number of Residues	5
Details	binding site for residue K C 602

Chain	Residue
C	ASP311
C	ASP313
C	HIS315
C	SER334
C	LEU335

---

site_id	AD3
Number of Residues	2
Details	binding site for residue SO4 C 603

Chain	Residue
C	ARG179
C	HOH709

---

site_id	AD4
Number of Residues	3
Details	binding site for residue ZN D 601

Chain	Residue
D	ASP313
D	HIS315
D	ASP404

---

site_id	AD5
Number of Residues	5
Details	binding site for residue K D 602

Chain	Residue
D	ASP311
D	ASP313
D	HIS315
D	SER334
D	LEU335

---

site_id	AD6
Number of Residues	2
Details	binding site for residue SO4 D 603

Chain	Residue
D	ARG179
D	HOH708

---

site_id	AD7
Number of Residues	3
Details	binding site for residue SO4 D 604

Chain	Residue
D	THR204
D	LYS205
D	HOH759

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:31061103

Chain	Residue	Details
A	HIS277
B	HIS277
C	HIS277
D	HIS277

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T

Chain	Residue	Details
A	ASP313
D	ASP313
D	HIS315
D	ASP404
A	HIS315
A	ASP404
B	ASP313
B	HIS315
B	ASP404
C	ASP313
C	HIS315
C	ASP404

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Polarizes the scissile carbonyl of the substrate => ECO:0000269|PubMed:32878973, ECO:0007744|PDB:6J6T

Chain	Residue	Details
A	TYR444
B	TYR444
C	TYR444
D	TYR444

---