Structure of PDB 1b3x Chain A

Receptor sequence
>1b3xA (length=302) Species: 69488 (Penicillium simplicissimum) [Search protein sequence]
QASVSIDAKFKAHGKKYLGTIGDQYTLTKNTKNPAIIKADFGQLTPENSM
KWDATEPNRGQFTFSGSDYLVNFAQSNGKLIRGHTLVWHSQLPGWVSSIT
DKNTLISVLKNHITTVMTRYKGKIYAWDVLNEIFNEDGSLRNSVFYNVIG
EDYVRIAFETARSVDPNAKLYINDYNLDSAGYSKVNGMVSHVKKWLAAGI
PIDGIGSQTHLGAGAGSAVAGALNALASAGTKEIAITELDIAGASSTDYV
NVVNACLNQAKCVGITVWGVADPDSWRSSSSPLLFDGNYNPKAAYNAIAN
AL
3D structure
PDB1b3x Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E132 N173 H210 E238 D240
Catalytic site (residue number reindexed from 1) E132 N173 H210 E238 D240
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 XYP A K51 H84 E132 Q208 E238 W268 W276 K51 H84 E132 Q208 E238 W268 W276
BS02 XYP A E47 N48 K51 Q91 E47 N48 K51 Q91
BS03 XYP A R119 Y120 K123 R119 Y120 K123
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
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:1b3x, PDBe:1b3x, PDBj:1b3x
PDBsum1b3x
PubMed10029534
UniProtP56588|XYNA_PENSI Endo-1,4-beta-xylanase

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