Structure of PDB 3pt1 Chain A

Receptor sequence
>3pt1A (length=464) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
HMTIPGRFMTIDKGTFGEYTASTRWPIIIQNAIDDLSKHQETEKSNGTKF
EQGEVIKKELKEFRQEIIDRVPLRPFTEEEIKIANVPLSFNEYLKKHPEV
NWGAVEWLFSEVYLYRRVNVLFQRQCEWAKFDIFNRLKQSTFESSFYGVV
ELALRYENLLPQLREMKQNDDILKVLFKEFIEISLWGNATDLSLLTNATL
EDIKSIQGAKARAASESKIVVNDTEKAWEVLTKARADANSREIRVDFVLD
NSGFELYADLMLAAFLLQSGLATKCIFHAKDIPYMVSDVMLKDFDILVHD
LRDREFFPSGEPSTKESRALDLFAGEMEKFVSSGKIEFREDSFWTTELDY
WNLDANETKYHGSILHKDLQKSNLVIFKGDLNYRKLTGDRKWPRTTKWET
AIGPLATNGITSLSLRTCKADVQVALPEGLDAKLSQEWEKENPGRGSWWC
CSGKWAVICFCSGI
3D structure
PDB3pt1 Structure and activity of a DUF89 protein from Saccharomyces cerevisiae revealed a novel family of carbohydrate phosphatases
ChainA
Resolution1.773 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.1.3.-
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 F6P A R23 E110 D254 G383 D384 L385 R388 K423 R24 E111 D250 G379 D380 L381 R384 K419
BS02 MG A D254 N255 D292 D250 N251 D288
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0046872 metal ion binding
GO:0097023 fructose 6-phosphate aldolase activity
GO:0103026 fructose-1-phosphatase activity
Biological Process
GO:0006974 DNA damage response
GO:0008150 biological_process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3pt1, PDBe:3pt1, PDBj:3pt1
PDBsum3pt1
PubMed
UniProtQ04371|ARMT1_YEAST Damage-control phosphatase YMR027W (Gene Name=YMR027W)

[Back to BioLiP]