Structure of PDB 1dlv Chain C

Receptor sequence
>1dlvC (length=389) Species: 350 (Zoogloea ramigera) [Search protein sequence]
SIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVI
LGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQI
ATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFY
GYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFI
VKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGA
AAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERA
GWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGAS
GARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL
3D structure
PDB1dlv Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase.
ChainC
Resolution2.29 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 COA C L148 H156 M157 R220 F235 A243 S247 A318 F319 H348 L145 H153 M154 R217 F232 A240 S244 A315 F316 H345
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:1dlv, PDBe:1dlv, PDBj:1dlv
PDBsum1dlv
PubMed10764581
UniProtP07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)

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