Structure of PDB 5efd Chain B

Receptor sequence
>5efdB (length=354) Species: 65673 (Bacillus sp. NG-27) [Search protein sequence]
VQPFAAQVASLADRYEESFDIGAAVEPHQLNGRQGKVLKHHYNSIVAENA
MKPISLQPEEGVFTWDGADAIVEFARKNNMNLRFHTLVWHNQVPDWFFLD
EEGNPMVEETNEAKRQANKELLLERLETHIKTVVERYKDDVTAWDVVNEV
VDDGTPNERGLRESVWYQITGDEYIRVAFETARKYAGEDAKLFINDYNTE
VTPKRDHLYNLVQDLLADGVPIDGVGHQAHIQIDWPTIDEIRTSMEMFAG
LGLDNQVTELDVSLYGWPPRPAFPTYDAIPQERFQAQADRYNQLFELYEE
LDADLSSVTFWGIADNHTWLDDRAREYNDGVGKDAPFVFDPNYRVKPAFW
RIID
3D structure
PDB5efd Small Glycols Discover Cryptic Pockets on Proteins for Fragment-Based Approaches.
ChainB
Resolution1.674 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E149 N195 H230 E259 D261
Catalytic site (residue number reindexed from 1) E149 N195 H230 E259 D261
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
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 MG B N292 R351 D354 N292 R351 D354
BS02 EDO B F4 A6 Y343 F4 A6 Y343
BS03 EDO B H230 Q232 W319 R323 H230 Q232 W319 R323
BS04 EDO B D153 V201 T202 P203 K204 D153 V201 T202 P203 K204
BS05 EDO B D206 N210 D206 N210
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031176 endo-1,4-beta-xylanase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5efd, PDBe:5efd, PDBj:5efd
PDBsum5efd
PubMed33570386
UniProtO30700

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