Structure of PDB 6ncx Chain D

Receptor sequence
>6ncxD (length=555) Species: 1432052 (Eisenbergiella tayi) [Search protein sequence]
MIRTFETHKIRKTAELSSALWNFHTIGTQGEEAVIQAPVPGCWENYPDTV
SYRGQASYSREFEAKGNIRLEFKGVSHTASVLVDGKPVGSHYNAYTPFDV
VLKDIRPGIHQLEVIADNSFGPDSALHVPNDYQSYGGISRGVVLEELGEA
YLSWIHFTPFLRKDGWYGKAEICVRNLSSGRLDGSVEVEIGKNSFAVLPI
VLEGEEEKSFSTEELPCPWAECWSPESPVLYLITAVLRTADDIIDRVGFR
EIRTEGKDILLNGRKLRIKGFCRHEDHPQFGCALPFSAMQHDLMLIKDLG
ANSIRTVHYPNDELFLDLCDEQGILVWEENHARGLSEENMRNPHFKQQCG
DCIREMITAHYNHPSIYIWGILNECASDTEYGRECYSEQYELIKSLDPYR
PRSSASCRFKTDICLGYPEVVSYNIYPKWYHDVPVEDYLDELYQWIQNES
EGTGKPFLITEIGAGAIYGYRTPAHVKWSEEYQVQALKEQLQAVFSREGC
SGVYIWQFCDVRVCDSWFGSRPRTMNNKGIVDEYRRPKLAYEVVKDSYRS
LGNYF
3D structure
PDB6ncx Selecting a Single Stereocenter: The Molecular Nuances That Differentiate beta-Hexuronidases in the Human Gut Microbiome.
ChainD
Resolution2.25 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.31: beta-glucuronidase.
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 ADA D D131 H312 R337 E378 Y430 Y434 E465 W510 R525 K532 D131 H308 R333 E374 Y426 Y430 E461 W506 R521 K528
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004566 beta-glucuronidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6ncx, PDBe:6ncx, PDBj:6ncx
PDBsum6ncx
PubMed30729778
UniProtA0A1E3AEY6

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