Structure of PDB 5ca3 Chain B

Receptor sequence
>5ca3B (length=759) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NADNYKNVINRTGAPQYMKDYDYDDHQRFNPFFDLGAWHGHLLPDGPNTM
GGFPGVALLTEEYINFMASNFDRLTVWQDGKKVDFTLEAYSIPGALVQKL
TAKDVQVEMTLRFATPRTSLLETKITSNKPLDLVWDGELLEKLEAKEGKP
LSDKTIAGEYPDYQRKISATRDGLKVTFGKVRATWDLLTSGESEYQVHKS
LPVQTEINGNRFTSKAHINGSTTLYTTYSHLLTAQEVSKEQMQIRDILAR
PAFYLTASQQRWEEYLKKGLTNPDATPEQTRVAVKAIETLNGNWRSPGGA
VKFNTVTPSVTGRWFSGNQTWPWNTWKQAFAMAHFNPDIAKENIRAVFSW
QIQPGDSVRPQDVGFVPDLIAWNLSPERGGDGGNWNERNTKPSLAAWSVM
EVYNVTQDKTWVAEMYPKLVAYHDWWLRNRDHNGNGVPEYGATRDKAHNT
ESGEMLFTVKKGDKEETQSGLNNYARVVEKGQYDSLEIPAQVAASWESGR
DDAAVFGFIDKEQLDKYVANGGKRSDWTVKFAENRSQDGTLLGYSLLQES
VDQASYMYSDNHYLAEMATILGKPEEAKRYRQLAQQLADYINTCMFDPTT
QFYYDVRIEDKPLANGCAGKPIVERGKGPEGWSPLFNGAATQANADAVVK
VMLDPKEFNTFVPLGTAALTNPAFGADIYWRGRVWVDQFWFGLKGMERYG
YRDDALKLADTFFRHAKGLTADGPIQENYNPLTGAQQGAPNFSWSAAHLY
MLYNDFFRK
3D structure
PDB5ca3 Crystal structure of the enzyme-product complex reveals sugar ring distortion during catalysis by family 63 inverting alpha-glycosidase.
ChainB
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.-
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004555 alpha,alpha-trehalase activity
GO:0015926 glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005991 trehalose metabolic process
GO:0005993 trehalose catabolic process
GO:0006974 DNA damage response
GO:0009313 oligosaccharide catabolic process
Cellular Component
GO:1902687 glucosidase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5ca3, PDBe:5ca3, PDBj:5ca3
PDBsum5ca3
PubMed27688023
UniProtP42592|YGJK_ECOLI Glucosidase YgjK (Gene Name=ygjK)

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