Structure of PDB 6jr8 Chain C

Receptor sequence
>6jr8C (length=812) Species: 376686 (Flavobacterium johnsoniae UW101) [Search protein sequence]
EQYLGNCTAYSVKGNKVVFSCANNSKIMLQLCSGEVVKIWASADGNFVRN
NESFAVIEEDLGWKGNVTVKEEPSTYEIFTEQLRIRVNKAPFQLQIFDKY
QKLLFSDYAEKGFVNDNGKIRTNKVLRNDEQFFGLGEKSGNLNRRGSAYK
MWNSDQPCYGVNEDPLYKSIPFFMSSYRYGIFFDNTYKTEFKFGSESNDY
YSFEAPAGQMVYYFMFGNDYKEIIQNYIALTGKPIMPPKWALGFSQCRGD
YTREDQAREIAAEFRKRKIPCDIIYQDIGWTEGLQDFDWRKNNYNNPKGM
VKDLSDMGFKMIVSQDPVISQANQQQWKEADALGHLVKDVRTGKSYDMPW
PWGGNCGVVDFTKPEVADWWGSYQQKPLNDGVRGFWTAMGEPAWSNEDAV
DRLNMKHHLGMHNEIHNVYGFTWDKVVTEQFYKHNPNKRIFQMTRAAYAG
LQRYTFGWSGDSGNGSNVLDGWKQMANQIPVGLSAGMGLIPFWTCDISGY
CGDIKDYDAMAELYVRWLQFGVFTPLSRAHHEGGNAVEPWKFGTEAENIS
RKSIELKYKLFPYLYTYAREAHDTGLPIMRALLLEYPNDKETFKLNGQFL
VGKELLVAPVVEQGAVTKDVYLPEGEWIDFNNCKTKYKGEQWITVDAPLN
TIPVFVKKGSIIPQMPVMQYIDEKKVYPVTFDIFPGNLNKETSFTFYEDD
GESRDYERDVFCKTKITSKASNEEIKITVGEREYKGYSPAGPRNFILKIH
ASNKPKDVFAGGEKLKNVKPHVLEKNIEADFTKINWSWNEAENVISVRIP
DSGKNAVITIKN
3D structure
PDB6jr8 Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31.
ChainC
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.20: alpha-glucosidase.
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 GLC C D301 W376 W410 R469 D485 Y524 H554 D277 W352 W386 R445 D461 Y500 H530
BS02 GLC C G273 I302 W376 Y524 E556 G557 G249 I278 W352 Y500 E532 G533
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004558 alpha-1,4-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6jr8, PDBe:6jr8, PDBj:6jr8
PDBsum6jr8
PubMed31552702
UniProtA5FBI1

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