Structure of PDB 6are Chain D

Receptor sequence
>6areD (length=398) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence]
GMSSLPAVYIVSSARTPVGSFLGSLSSLTAPQLGAHAIKAALAKVDGLKP
SDVQEVFFGNVISANVGQNPARQCALGAGLEESTICTTVNKVCASGLKAI
ILGAQTIMTGNADVVVAGGTESMSNAPHYLPNLRTGAKYGHQSLVDGIMK
DGLTDAGKQELMGLQAEECAQDHGFSREQQDEYAIRTYEKAQAAQKAGLF
DEEIAPIQLPGFRKPDVTVTQDEEPKNLNPEKLRAIKPAFIPGSGTVTAP
NSSPLNDGAAAVVLVSEAKLKELNLKPVAKILGWGDAAQQPSKFTTAPAL
AIPKALKHAGVGQDAIDAFEINEAFSVVALANMKLLGIPEEKVNLHGGAV
AIGHPIGASGARILTTLLGVLKAKKGKLGCAGICNGGGGASALVVELL
3D structure
PDB6are Structure of Aspergillus fumigatus Cytosolic Thiolase: Trapped Tetrahedral Reaction Intermediates and Activation by Monovalent Cations
ChainD
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C92 H354 C384 G386
Catalytic site (residue number reindexed from 1) C93 H354 C384 G386
Enzyme Commision number 2.3.1.9: acetyl-CoA C-acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 COA D C92 L152 M161 Y187 N227 N229 I236 A249 P250 S253 H354 C93 L153 M162 Y188 N227 N229 I236 A249 P250 S253 H354
Gene Ontology
Molecular Function
GO:0003985 acetyl-CoA C-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
Biological Process
GO:0006635 fatty acid beta-oxidation
GO:0006696 ergosterol biosynthetic process
GO:0016126 sterol biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6are, PDBe:6are, PDBj:6are
PDBsum6are
PubMed
UniProtQ4WCL5|ER10B_ASPFU Acetyl-CoA acetyltransferase erg10B, cytosolic (Gene Name=erg10B)

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