Structure of PDB 6vo5 Chain A Binding Site BS02

Receptor Information

>6vo5 Chain A (length=322) Species: 9606 (Homo sapiens)

KKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGY
KGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGF
CTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCR
GFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATV
GYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPT
VLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMAIEAQQ
KFKINKQHARRVYEILRLLVTD

Ligand information

• Ligand ID: CO6
• InChI: InChI=1S/C25H42N7O17P3S/c1-13(2)24(37)53-8-7-27-15(33)5-6-28-22(36)19(35)25(3,4)10-46-52(43,44)49-51(41,42)45-9-14-18(48-50(38,39)40)17(34)23(47-14)32-12-31-16-20(26)29-11-30-21(16)32/h11-14,17-19,23,34-35H,5-10H2,1-4H3,(H,27,33)(H,28,36)(H,41,42)(H,43,44)(H2,26,29,30)(H2,38,39,40)/t14-,17-,18-,19+,23-/m1/s1
• InChIKey: AEWHYWSPVRZHCT-NDZSKPAWSA-N
• SMILES:
  CACTVS 3.341: CC(C)C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
  CACTVS 3.341: CC(C)C(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
  ACDLabs 10.04: O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)C(C)C
  OpenEye OEToolkits 1.5.0: CC(C)C(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
  OpenEye OEToolkits 1.5.0: CC(C)C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
• Formula: C25 H42 N7 O17 P3 S
• Name: ISOBUTYRYL-COENZYME A;
  IB-CO6
• PDB chain: 6vo5 Chain A Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6vo5 Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4
• Resolution: 1.6 Å
• Binding residue (original residue number in PDB): V238 M241 L242 I243 Q248 G249 G251 G253 A254 P278 S279 S281 Y282 K284 L285 F288
• Binding residue (residue number reindexed from 1): V219 M222 L223 I224 Q229 G230 G232 G234 A235 P259 S260 S262 Y263 K265 L266 F269
• Annotation score: 3

Enzymatic activity

• Catalytic site (original residue number in PDB): M241 E276
• Catalytic site (residue number reindexed from 1): M222 E257
• Enzyme Commision number: 2.3.1.48: histone acetyltransferase.

Gene Ontology

Molecular Function

• GO:0004402 histone acetyltransferase activity
• GO:0042393 histone binding

Biological Process

• GO:0006325 chromatin organization
• GO:0031509 subtelomeric heterochromatin formation

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:6vo5, PDBe:6vo5, PDBj:6vo5
• PDBsum: 6vo5
• UniProt: O14929|HAT1_HUMAN Histone acetyltransferase type B catalytic subunit (Gene Name=HAT1)