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 | 939 |
Details | Region: {"description":"Histone deacetylase"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"31061103","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"32878973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J6T","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Site: {"description":"Polarizes the scissile carbonyl of the substrate","evidences":[{"source":"PubMed","id":"32878973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J6T","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |