3C0Y

Crystal structure of catalytic domain of human histone deacetylase HDAC7

Replaces:  2NVRReplaces:  2I4Y

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	HOH289
A	ASP707
A	HIS709
A	ASP801

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	CYS533
A	CYS535
A	HIS541
A	CYS618

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 904

Chain	Residue
A	ASP707
A	HIS709
A	SER728
A	LEU729
A	ASP705

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 905

Chain	Residue
A	HOH41
A	HOH52
A	PHE718
A	ASP721
A	VAL724
A	PHE755

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 403

Chain	Residue
B	HOH142
B	HOH352
B	ASP707
B	HIS709
B	ASP801

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 404

Chain	Residue
B	CYS533
B	CYS535
B	HIS541
B	CYS618

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 904

Chain	Residue
B	ASP705
B	ASP707
B	HIS709
B	SER728
B	LEU729

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 905

Chain	Residue
B	HOH17
B	HOH34
B	PHE718
B	ASP721
B	VAL724
B	PHE755

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 405

Chain	Residue
C	HOH291
C	ASP707
C	HIS709
C	ASP801

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 406

Chain	Residue
C	CYS533
C	CYS535
C	HIS541
C	CYS618

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 904

Chain	Residue
C	ASP705
C	ASP707
C	HIS709
C	SER728
C	LEU729

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 905

Chain	Residue
C	HOH45
C	HOH190
C	PHE718
C	ASP721
C	VAL724
C	PHE755

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q8C2B3

Chain	Residue	Details
A	HIS670
B	HIS670
C	HIS670

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:18285338

Chain	Residue	Details
A	CYS533
C	CYS535
C	HIS541
C	CYS618
A	CYS535
A	HIS541
A	CYS618
B	CYS533
B	CYS535
B	HIS541
B	CYS618
C	CYS533

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	SITE: Contributes to catalysis => ECO:0000269|PubMed:18285338

Chain	Residue	Details
A	HIS843
B	HIS843
C	HIS843

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER486
B	SER486
C	SER486

---

site_id	SWS_FT_FI5
Number of Residues	9
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER487
A	SER507
A	SER595
B	SER487
B	SER507
B	SER595
C	SER487
C	SER507
C	SER595

---