Structure of PDB 1dm3 Chain C

Receptor sequence
>1dm3C (length=389) Species: 350 (Zoogloea ramigera) [Search protein sequence]
SIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVI
LGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQI
ATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFY
GYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFI
VKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGA
AAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERA
GWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGAS
GARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL
3D structure
PDB1dm3 Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C89 H348 C378 G380
Catalytic site (residue number reindexed from 1) C86 H345 C375 G377
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 ACO C C89 L148 H156 M157 R220 S227 M228 A243 G244 S247 M288 A318 F319 H348 C378 I379 C86 L145 H153 M154 R217 S224 M225 A240 G241 S244 M285 A315 F316 H345 C375 I376
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
Biological Process
GO:0042619 poly-hydroxybutyrate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1dm3, PDBe:1dm3, PDBj:1dm3
PDBsum1dm3
PubMed10764581
UniProtP07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)

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