Structure of PDB 3ser Chain A

Receptor sequence
>3serA (length=370) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KIEEGKLVIWINGDKGYNGLAEVGHKFEHDTGIKVTVEHPDKLEEKFPQV
AATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYN
GKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFN
LQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIK
NKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTF
KGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINA
ASGRQTVDAALAAAQTNAAA
3D structure
PDB3ser An approach to crystallizing proteins by metal-mediated synthetic symmetrization.
ChainA
Resolution2.35 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 GLC A D15 K16 E112 Y156 F157 W231 D14 K15 E111 Y155 F156 W230
BS02 GLC A W63 D66 R67 E154 P155 Y156 W341 W62 D65 R66 E153 P154 Y155 W340
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0015144 carbohydrate transmembrane transporter activity
GO:1901982 maltose binding
Biological Process
GO:0006974 DNA damage response
GO:0008643 carbohydrate transport
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: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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ser, PDBe:3ser, PDBj:3ser
PDBsum3ser
PubMed21898649
UniProtP0AEX9|MALE_ECOLI Maltose/maltodextrin-binding periplasmic protein (Gene Name=malE)

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