Structure of PDB 7dd9 Chain G

Receptor sequence
>7dd9G (length=1129) Species: 83333,284812 [Search protein sequence]
TLFPVLNNTPVGKQVDSIYESRLDQFLSEGQYRDFNLPSVYDHARIDNPS
GDVNNDLSKGFVDLKVYRVPDLSRPSFNEVVGHKKFDETASKGDTFGPSW
ATFWFEVHIRLPKSWAKYEQVIFQWNCDNEGLVYSQDGVPLQAFSGSERT
DFILPDSWKTTEDTFYIEMACNGMFGTGAGSQIAPPDPNRYFTLTKADLV
APNLPAMALAYDFLLMQQCVKQLPSNCWQKYKARQICNDIMNTFHPNDLS
TINECRNLAKAFLGNDIDSEAVFEKNNDKANVFAIGHCHIDTAWLWPFAE
TRRKIVRSWATQMNIMDRYPEYQFVCSQALQYLWLKEDHPDVFEKLKEYV
NQNKFIPIGGSWVEHDTNIPNGESLIRQFLLGQHFFEKEFGVRCRTFWLP
DTFGYSSQIPQICRLCGMDRFLTQKLSWNNINSFPTSTFNWVALDGSQVI
CHMPPANTYTADTNVNDVLHSIDQHKNLVNDQAGLLVFGIGDGGGGPTPE
MLEKLRRCKGIANTVGYLPNVKLGNTVDEFFDGILKRTNAGQTLPSWNGE
LYFEFHRGTYTTQAELKKLMRKVEIALHDAEYVSTLASIFSKDYSYPKES
LQDLWRDTLLCQFHDVLPGSCIEMVYKDAIPIMSKVLKNTEALLWQAIEQ
LGFKKASSSDNKEQLCLLNTLPWNVRGVITETEENKLVYFESCDGKGILT
AAHTSLKHPAAAYQKDDNFILVNDHLRVTIAPNGLILSLFDLHKEREILD
LKSGKNHAGANQYVLFEDTPLSWQAWDTEVFSLEKYEVLDKGKVSIKESG
PLRASVVVDIPISELSHMKATISLEGYNDCSEFTGVNFTCEVDWHESCKF
LKVEFPVDIHSEFASYETQFGITKRPTHYNTSWDVAKFEVCHQKFADYSD
FTYGVSVLNDCKYGFSTHGNLMRLSLLRSPKQPDAHADMGKHTIRYAVYP
HSKPLDSSTVRAAHKFNSNFRLLTRASDTANLDIFDAFQLVGEPNVILSH
IKMAEKGKSIILRVYESLGGKSRARLVIKSLTVASVTKCNGLEEDLEELC
TLKSNDYYEVPIELRAFEIATFKVNLGFKSVACNTCLKIIRNDSFHCTKC
FDFDVCRDCYAKQAFLHPCPKPHFVLVRS
3D structure
PDB7dd9 Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.
ChainG
Resolution2.4 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 3.2.1.24: alpha-mannosidase.
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 ZN G H290 D292 D402 H615 H289 D291 D401 H614
BS02 ZN G C2076 C2079 H2096 C2098 C1097 C1100 H1117 C1119
BS03 ZN G C2062 C2085 C2088 C1083 C1106 C1109
Gene Ontology
Molecular Function
GO:0004559 alpha-mannosidase activity
GO:0004571 mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
GO:0052767 mannosyl-oligosaccharide 1,6-alpha-mannosidase activity
GO:0052768 mannosyl-oligosaccharide 1,3-alpha-mannosidase activity
GO:1901982 maltose binding
Biological Process
GO:0006013 mannose metabolic process
GO:0006974 DNA damage response
GO:0008643 carbohydrate transport
GO:0009313 oligosaccharide catabolic process
GO:0015768 maltose transport
GO:0034219 carbohydrate transmembrane transport
GO:0034289 detection of maltose stimulus
GO:0042956 maltodextrin transmembrane transport
GO:0055085 transmembrane transport
GO:0060326 cell chemotaxis
Cellular Component
GO:0000328 fungal-type vacuole lumen
GO:0000329 fungal-type vacuole membrane
GO:0005737 cytoplasm
GO:0005773 vacuole
GO:0005829 cytosol
GO:0016020 membrane
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space
GO:0043190 ATP-binding cassette (ABC) transporter complex
GO:0055052 ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
GO:1990060 maltose transport complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7dd9, PDBe:7dd9, PDBj:7dd9
PDBsum7dd9
PubMed34169534
UniProtP0AEX9|MALE_ECOLI Maltose/maltodextrin-binding periplasmic protein (Gene Name=malE);
Q9P792;
Q9UT61|MAN1_SCHPO Alpha-mannosidase (Gene Name=ams1)

[Back to BioLiP]