Structure of PDB 1asq Chain A Binding Site BS03

Receptor Information
>1asq Chain A (length=552) Species: 3665 (Cucurbita pepo var. melopepo) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SQIRHYKWEVEYMFWAPNCNENIVMGINGQFPGPTIRANAGDSVVVELTN
KLHTEGVVIHWHGILQRGTPWADGTASISQCAINPGETFFYNFTVDNPGT
FFYHGHLGMQRSAGLYGSLIVDPPQGKKEPFHYDGEINLLLSDWWHQSIH
KQEVGLSSKPIRWIGEPQTILLNGRGQFDCSIAAKYDSNLEPCKLKGSES
CAPYIFHVSPKKTYRIRIASTTALAALNFAIGNHQLLVVEADGNYVQPFY
TSDIDIYSGESYSVLITTDQNPSENYWVSVGTRARHPNTPPGLTLLNYLP
NSVSKLPTSPPPQTPAWDDFDRSKNFTYRITAAMGSPKPPVKFNRRIFLL
NTQNVINGYVKWAINDVSLALPPTPYLGAMKYNLLHAFDQNPPPEVFPED
YDIDTPPTNEKTRIGNGVYQFKIGEVVDVILQNANMMKENLSETHPWHLH
GHDFWVLGYGDGKFSAEEESSLNLKNPPLRNTVVIFPYGWTAIRFVADNP
GVWAFHCHIEPHLHMGMGVVFAEGVEKVGRIPTKALACGGTAKSLINNPK
NP
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain1asq Chain A Residue 556 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1asq X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms.
Resolution2.32 Å
Binding residue
(original residue number in PDB)
H62 H104 H508
Binding residue
(residue number reindexed from 1)
H62 H104 H508
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H60 H62 H104 H106 H445 H448 H450 H506 C507 H508 I509 H512 M517
Catalytic site (residue number reindexed from 1) H60 H62 H104 H106 H445 H448 H450 H506 C507 H508 I509 H512 M517
Enzyme Commision number 1.10.3.3: L-ascorbate oxidase.
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0008447 L-ascorbate oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Cellular Component
GO:0005576 extracellular region
GO:0009506 plasmodesma

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:1asq, PDBe:1asq, PDBj:1asq
PDBsum1asq
PubMed8478945
UniProtP37064|ASO_CUCPM L-ascorbate oxidase

[Back to BioLiP]