Structure of PDB 1nl7 Chain B

Receptor sequence
>1nl7B (length=390) Species: 350 (Zoogloea ramigera) [Search protein sequence]
PSIVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEV
ILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQ
IATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAF
YGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPF
IVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDG
AAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALER
AGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGA
SGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL
3D structure
PDB1nl7 Crystal structures of Z. ramigera biosynthetic thiolase
ChainB
Resolution1.903 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) C87 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 COA B C89 L148 H156 M157 R220 S227 M228 S247 F319 H348 C87 L146 H154 M155 R218 S225 M226 S245 F317 H346
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:1nl7, PDBe:1nl7, PDBj:1nl7
PDBsum1nl7
PubMed
UniProtP07097|THIL_SHIZO Acetyl-CoA acetyltransferase (Gene Name=phaA)

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