Structure of PDB 2ibu Chain A Binding Site BS01

Receptor Information

>2ibu Chain A (length=391) Species: 9606 (Homo sapiens)

PTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEV
KEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMA
SQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTD
VYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVI
PVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTL
NDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMV
LKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHP
IGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL

Ligand information

• Ligand ID: COA
• InChI: InChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
• InChIKey: RGJOEKWQDUBAIZ-IBOSZNHHSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O
  CACTVS 3.341: CC(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)[C@@H](O)C(=O)NCCC(=O)NCCS
  OpenEye OEToolkits 1.5.0: CC(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)[C@H](C(=O)NCCC(=O)NCCS)O
  CACTVS 3.341: CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCS
  ACDLabs 10.04: O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
• Formula: C21 H36 N7 O16 P3 S
• Name: COENZYME A
• ChEMBL: CHEMBL1213327
• DrugBank: DB01992
• ZINC: ZINC000008551087
• PDB chain: 2ibu Chain A Residue 6001

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2ibu Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): L184 H192 M193 Y219 R258 V259 D260 V264 L267 F271 A280 A281 S284 F325 A355 F356 H385
• Binding residue (residue number reindexed from 1): L148 H156 M157 Y183 R222 V223 D224 V228 L231 F235 A244 A245 S248 F289 A319 F320 H349
• Annotation score: 3

Enzymatic activity

• Catalytic site (original residue number in PDB): C126 H385 C413 G415
• Catalytic site (residue number reindexed from 1): C90 H349 C377 G379
• Enzyme Commision number: 2.3.1.9: acetyl-CoA C-acetyltransferase.

Gene Ontology

Molecular Function

• GO:0003985 acetyl-CoA C-acetyltransferase activity
• GO:0003988 acetyl-CoA C-acyltransferase activity
• GO:0016453 C-acetyltransferase activity
• GO:0016746 acyltransferase activity
• GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
• GO:0019899 enzyme binding
• GO:0030955 potassium ion binding
• GO:0034736 cholesterol O-acyltransferase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding
• GO:0120225 coenzyme A binding

Biological Process

• GO:0001889 liver development
• GO:0006085 acetyl-CoA biosynthetic process
• GO:0006550 isoleucine catabolic process
• GO:0006631 fatty acid metabolic process
• GO:0006635 fatty acid beta-oxidation
• GO:0009725 response to hormone
• GO:0014070 response to organic cyclic compound
• GO:0015936 coenzyme A metabolic process
• GO:0015937 coenzyme A biosynthetic process
• GO:0042594 response to starvation
• GO:0046356 acetyl-CoA catabolic process
• GO:0046952 ketone body catabolic process
• GO:0060612 adipose tissue development
• GO:0072229 metanephric proximal convoluted tubule development
• GO:1902224 ketone body metabolic process
• GO:1902860 propionyl-CoA biosynthetic process

Cellular Component

• GO:0005739 mitochondrion
• GO:0005759 mitochondrial matrix
• GO:0005783 endoplasmic reticulum
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:2ibu, PDBe:2ibu, PDBj:2ibu
• PDBsum: 2ibu
• PubMed: 17371050
• UniProt: P24752|THIL_HUMAN Acetyl-CoA acetyltransferase, mitochondrial (Gene Name=ACAT1)