Structure of PDB 3vfj Chain A

Receptor sequence

>3vfjA (length=377) Species: 83333 (Escherichia coli K-12)

KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQV
AATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYN
GKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFN
LQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIK
NKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTF
KGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINA
ASGRQTVDEALKDAQTNAAAAAGCKAA

3D structure

• PDB: 3vfj Structure of the complex between teicoplanin and a bacterial cell-wall peptide: use of a carrier-protein approach.
• Chain: A
• Resolution: 2.05 Å

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	peptide	A	K375 A376 A377	K375 A376 A377
BS02	ZN	A	E288 E291	E288 E291
BS03	ZN	A	E359 D363	E359 D363
BS04	ZN	A	E172 D177	E172 D177

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

External links

• PDB: RCSB:3vfj, PDBe:3vfj, PDBj:3vfj
• PDBsum: 3vfj
• PubMed: 23519660
• UniProt: P0AEX9|MALE_ECOLI Maltose/maltodextrin-binding periplasmic protein (Gene Name=malE)