Structure of PDB 3vpl Chain A

Receptor sequence
>3vplA (length=324) Species: 678 (Vibrio sp.) [Search protein sequence]
LDGVLVPESGILVSVGQDVDSVNDYASALGTIPAGVTNYVGIVNLDGLNS
DADAGAGRNNIAELANAYPTSALVVGVSMNGEVDAVASGRYNANIDTLLN
TLAGYDRPVYLRWAYEVDGPWNGHSPSGIVTSFQYVHDRIIALGHQAKIS
LVWQVASYCPTPGGQLDQWWPGSEYVDWVGLSYFAPQDCNWDRVNEAAQF
ARSKGKPLFLNESTPQRYQVADLTYSADPAKGTNRQSKTSQQLWDEWFAP
YFQFMSDNSDIVKGFTYINADWDSQWRWAAPYNEGYWGDSRVQANALIKS
NWQQEIAKGQYINHSETLFETLGY
3D structure
PDB3vpl Mechanistic insights into the 1,3-xylanases: useful enzymes for manipulation of algal biomass
ChainA
Resolution1.2 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 3.2.1.32: endo-1,3-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 BXF A Y115 E116 F184 E212 W272 W287 Y115 E116 F184 E212 W272 W287
BS02 XYP A Q17 Y39 Y115 R277 Q17 Y39 Y115 R277
BS03 XYP A G41 D46 N80 G41 D46 N80
BS04 BXF A R277 W278 E284 R277 W278 E284
BS05 XYP A R277 E284 R277 E284
BS06 DNX A P229 A230 E284 G285 P229 A230 E284 G285
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

View graph for
Molecular Function
External links
PDB RCSB:3vpl, PDBe:3vpl, PDBj:3vpl
PDBsum3vpl
PubMed
UniProtD5MP61|3XYN1_VIBSX Beta-1,3-xylanase XYL4 (Gene Name=xyl4)

[Back to BioLiP]