Structure of PDB 1m1o Chain B

Receptor sequence
>1m1oB (length=390) Species: 350 (Zoogloea ramigera) [Search protein sequence]
PSIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEV
ILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLAGSGLRAVALGMQQ
IATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAF
YGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPF
IVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDG
AAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALER
AGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGA
SGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL
3D structure
PDB1m1o The catalytic cycle of biosynthetic thiolase: A conformational journey of an acetyl group through four binding modes and two oxyanion holes
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A89 H348 C378 G380
Catalytic site (residue number reindexed from 1) A87 H346 C376 G378
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 CAA B L88 A89 L148 H156 M157 R220 S227 M228 L231 A243 G244 S247 A318 H348 C378 I379 G380 L86 A87 L146 H154 M155 R218 S225 M226 L229 A241 G242 S245 A316 H346 C376 I377 G378
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:1m1o, PDBe:1m1o, PDBj:1m1o
PDBsum1m1o
PubMed12501183
UniProtP07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)

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