Structure of PDB 1wa6 Chain X

Receptor sequence
>1wa6X (length=298) Species: 4102 (Petunia x hybrida) [Search protein sequence]
ENFPIISLDKVNGVERAATMEMIKDACENWGFFELVNHGIPREVMDTVEK
MTKGHYKKCMEQRFKELVASKALEGVQAEVTDMDWESTFFLKHLPISNIS
EVPDLDEEYREVMRDFAKRLEKLAEELLDLLCENLGLEKGYLKNAFYGSK
GPNFGTKVSNYPPCPKPDLIKGLRAHTDAGGIILLFQDDKVSGLQLLKDG
QWIDVPPMRHSIVVNLGDQLEVITNGKYKSVMHRVIAQKDGARMSLASFY
NPGSDAVIYPAPALVQVYPKFVFDDYMKLYAGLKFQAKEPRFEAMKAM
3D structure
PDB1wa6 Crystal Structure and Mechanistic Implications of 1-Aminocyclopropane-1-Carboxylic Acid Oxidase (the Ethyling Forming Enzyme)
ChainX
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H177 D179 H234
Catalytic site (residue number reindexed from 1) H176 D178 H233
Enzyme Commision number 1.14.17.4: aminocyclopropanecarboxylate oxidase.
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 FE2 X H177 D179 H234 H176 D178 H233
Gene Ontology
Molecular Function
GO:0009815 1-aminocyclopropane-1-carboxylate oxidase activity
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0031418 L-ascorbic acid binding
GO:0046872 metal ion binding
Biological Process
GO:0002238 response to molecule of fungal origin
GO:0009693 ethylene biosynthetic process
GO:0009805 coumarin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1wa6, PDBe:1wa6, PDBj:1wa6
PDBsum1wa6
PubMed15489165
UniProtQ08506|ACCO1_PETHY 1-aminocyclopropane-1-carboxylate oxidase 1 (Gene Name=ACO1)

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