Structure of PDB 7vqo Chain D

Receptor sequence
>7vqoD (length=1180) Species: 83333,759272 [Search protein sequence]
GGETFDVKGPRPNDYPLRAPKPVGQLISHIYKDRIAQFYNGGQYEHQNLR
AMMKEDSVSGEPHVQLWVWHAPGQTRPSFEEAVSNQFVKTNVGEWFGPSW
TTHWFRVVLTVPEHLQNKRLLEFHWDSNSEGLVWSEDGKPLQGLTGGGER
VEWILPDSFRDGKEHTIYIEMACNRMFGNAPGGDSIQPPDPNKYFRLDKA
EIVAIDPDARQLWIDIWILQDAAREFPGDSWESHKALQVCNEIIEAFELG
NRESLKKCRKIAEQYLGPNVDSPNVYNSGKEPLVYAIGHCHIDSCWLWPF
AETKRKVVRSWSSQCDLMDRYPELNFVCSQAQQYKWLKQLYPYAFERVKK
KVAEGRFHPIGGSWVEHDTNMPSGESLVRQFLYGQRFYESNFGKRCKTFW
LPDTFGYSAQLPQLCRLAGMTRFLTQKLSWNNINRFPHTTFNWVALDGSQ
VICHMPPSETYTAEAHFGDVKRSMSQHKSLDQDNTSLLVFGKGDGGGGPT
WVQIEKLRRCRGISDTVGLLPRVHMGSSVDDFFDRLERKADTFVTWYGEL
YFELHRGTYTTQAKNKKNNRRAEAKLRDLELLATIASVQDKSYKYPKEEF
DAMWENVLLCQFHDCLPGSSIEMAYRESDQMYADVFSTAEKIMKGVSQVL
GLEPALNHMSTTNTVALNTLPWPRRELVKISEKEAAVAHGTGPFLKLQKL
ETTKPLVTLRQVTKGAFVLENSQLRVHVEKGVITSLYDKQANREVIPKGQ
KANQYVIFDDKPLYWQAWDVEVYHLDTRKELPSGETEVHENTPHRVSVVT
RTKVSDKSHIQTIIALNGAVEGEQSWVEVQSKVDWHETMKFLKVEFPVDV
RNTEASYETAFGIVRRPTHYNTSWDMAKFEVCAHRWADLSEYGYGVSILN
DSKYGFATAGQTMRLSLLRSPKAPDAHADMGTHHIRWAILPHQGSLSHVT
IRKAFEFNNPTKLYSSPDAAALVAAPPPVWLTPDSSPAIVLDTVKRGEDD
EDVSRGELPARKGQSVILRMYDSLGGLARGTVVTTWPLKKVCKVNLLEDD
LEVVPWENGRFTVELRPFEVASYRLVLALEATFVRDTVQDGTVLAPNHLF
EQTWVLRNTGKVAWPAGCSVKFVGGDYMGRVAVQPGEEAPFTVLLRTPYR
ACRVISHWRLTTPKGTKFGHRLWCDVVVEK
3D structure
PDB7vqo Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1
ChainD
Resolution2.19 Å
3D
structure
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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 D H292 D294 D404 H614 H291 D293 D403 H613
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004559 alpha-mannosidase activity
GO:0005515 protein binding
GO:0015144 carbohydrate transmembrane transporter activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0046872 metal ion binding
GO:1901982 maltose binding
Biological Process
GO:0005975 carbohydrate metabolic 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:0000329 fungal-type vacuole membrane
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:7vqo, PDBe:7vqo, PDBj:7vqo
PDBsum7vqo
PubMed
UniProtG0SE85;
G0SGP6;
P0AEX9|MALE_ECOLI Maltose/maltodextrin-binding periplasmic protein (Gene Name=malE)

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