Structure of PDB 5gw7 Chain A

Receptor sequence
>5gw7A (length=758) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NADNYKNVINRTGAPQYMKDYDYDDHQRFNPFFDLGAWHGHLLPDGPNTM
GGFPGVALLTEEYINFMASNFDRLTVWQDGKKVDFTLEAYSIPGALVQKL
TAKDVQVEMTLRFATPRTSLLETKITSNKPLDLVWDGELLEKLEAKEGKP
LSDKTIAGEYPDYQRKISATRDGLKVTFGKVRATWDLLTSGESEYQVHKS
LPVQTEINGNRFTSKAHINGSTTLYTTYSHLLTAQEVSKEQMQIRDILAR
PAFYLTASQQRWEEYLKKGLTNPDATPEQTRVAVKAIETLNGNWRSPGGA
VKFNTVTPSVTGRWFSGNQTWPWDTWKQAFAMAHFNPDIAKENIRAVFSW
QIQPGDSVRPQDVGFVPDLIAWNLSPERGGDGGNWNERNTKPSLAAWSVM
EVYNVTQDKTWVAEMYPKLVAYHDWWLRNRDHNGNGVPEYGATRDKAHNT
ESGEMLFTVKKGDKEETQSGLNNYARVVEKGQYDSLEIPAQVAASWESGR
DDAAVFGFIDKEQLDKYVANGGKRSDWTVKFAENRSQDGTLLGYSLLQES
VDQASYMYSDNHYLAEMATILGKPEEAKRYRQLAQQLADYINTCMFDPTT
QFYYDVRIEDKPLANGCAGKPIVERGKGPEGWSPLFNGAATQANADAVVK
VMLDPKEFNTFVPLGTAALTNPAFGADIYWRGRVWVDQFWFGLKGMERYG
YRDDALKLADTFFRHAKGLTADGPIQANYNPLTGAQQGAPNFSWSAAHLY
MLYNDFFR
3D structure
PDB5gw7 Crystal structure of the enzyme-product complex reveals sugar ring distortion during catalysis by family 63 inverting alpha-glycosidase
ChainA
Resolution2.2 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.-
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 GAL A W321 D368 K391 W496 D501 W321 D368 K391 W496 D501
BS02 GLC A D463 K464 D463 K464
BS03 CA A D431 N433 N435 V437 E439 E549 D431 N433 N435 V437 E439 E549
BS04 BGC A P308 F315 W321 W323 D324 G499 D501 F742 W744 P308 F315 W321 W323 D324 G499 D501 F742 W744
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5gw7, PDBe:5gw7, PDBj:5gw7
PDBsum5gw7
PubMed27688023
UniProtP42592|YGJK_ECOLI Glucosidase YgjK (Gene Name=ygjK)

[Back to BioLiP]