Structure of PDB 5tcv Chain A

Receptor sequence
>5tcvA (length=299) Species: 4102 (Petunia x hybrida) [Search protein sequence]
NFPIISLDKVNGVERAATMEMIKDACENWGFFELVNHGIPREVMDTVEKM
TKGHYKKCMEQRFKELVASKALEGVQAEVTDMDWESTFFLKHLPISNISE
VPDLDEEYREVMRDFAKRLEKLAEELLDLLCENLGLEKGYLKNAFYGSKG
PNFGTKVSNYPPCPKPDLIKGLRAHTDAGGIILLFQDDKVSGLQLLKDGQ
WIDVPPMRHSIVVNLGDQLEVITNGKYKSVMHRVIAQKDGARMSLASFYN
PGSDAVIYPAPALVEKQVYPKFVFDDYMKLYAGLKFQAKEPRFEAMKAM
3D structure
PDB5tcv ACC oxidase complex with substrate 1-aminocyclopropane-1-carboxylic acid
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K158 H177 D179 H234
Catalytic site (residue number reindexed from 1) K156 H175 D177 H232
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 1AC A H177 D179 L195 H234 H175 D177 L193 H232
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:5tcv, PDBe:5tcv, PDBj:5tcv
PDBsum5tcv
PubMed
UniProtQ08506|ACCO1_PETHY 1-aminocyclopropane-1-carboxylate oxidase 1 (Gene Name=ACO1)

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