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Structure of PDB 7fe4 Chain C

Receptor sequence
>7fe4C (length=659) Species: 376686 (Flavobacterium johnsoniae UW101) [Search protein sequence]
HQDPWKLSADKPDSNNYYGETVANGMIGIISSPEPLKVKEVVLAGTYDIY
KRGRVSSFIPNYNLLNMKLAFNGESVQTYNINNYKQELDMRNGAFTGSFQ
FKDLATVTYSYYALRHLPHCIMMVVNINTQKDTEINVENLLETPSSLNNQ
QNYFQNITNTHVNIPLLTSVAFTPTGRSKIAVSNTFLFDEGKKLQPEILH
RMNDADMHAMSFDKKIKAGKTYSFALIGSLISSDHINDPYNEAERLTIYA
ALEGKSRLLNRHMQEWNSLWQSDIQVEGDPQAQQDIRSMLYHLYSFTRKS
TSLSPSPMGLSGLGYNGHVFWDTEIWMFPPMLLLHPEIAKSMIEYRYQRL
DAARKKAAIYGYDGAMFPWESADSGAEETPVNALTGAFEHHVTGDVAIAA
WQYYLVTGDKEWLKEKGWPILKATAEFWASRVEKNDKGEYEIKNVVAADE
WAENIDNNAYTNGTAIRNLQYASKCATVLGVIAPKEWTLIADKILISKMS
NGVTREHDSYTDQNIKQADANLLAYPLKLITDKEQIERDLKYYQTKIPQS
DTPAMTQAIFSLLYSRLEDSDQAYHWFKDAYQPNLNPPFRVISECKGGTN
PYFSTGAGGVLQAVIMGFGGLDIDAAGGIKQVKSVLPKNWKKLTITGIGI
EKKTFVLTH
3D structure
PDB7fe4 Structure of a bacterial alpha-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.
ChainC
Resolution1.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 BGC C E275 R279 E253 R257
BS02 BGC C N466 D478 N444 D456
BS03 BGC C P329 Y337 F342 W343 D344 E472 K538 Q539 M577 P307 Y315 F320 W321 D322 E450 K516 Q517 M555
BS04 BGC C R74 W391 E392 P402 A405 E472 R52 W369 E370 P380 A383 E450
BS05 BGC C W473 K538 D573 W451 K516 D551
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016787 hydrolase activity
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process

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External links

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