Structure of PDB 1bg4 Chain A

Receptor sequence
>1bg4A (length=302) Species: 69488 (Penicillium simplicissimum) [Search protein sequence]
QASVSIDAKFKAHGKKYLGTIGDQYTLTKNTKNPAIIKADFGQLTPENSM
KWDATEPNRGQFTFSGSDYLVNFAQSNGKLIRGHTLVWHSQLPGWVSSIT
DKNTLISVLKNHITTVMTRYKGKIYAWDVLNEIFNEDGSLRNSVFYNVIG
EDYVRIAFETARSVDPNAKLYINDYNLDSAGYSKVNGMVSHVKKWLAAGI
PIDGIGSQTHLGAGAGSAVAGALNALASAGTKEIAITELDIAGASSTDYV
NVVNACLNQAKCVGITVWGVADPDSWRSSSSPLLFDGNYNPKAAYNAIAN
AL
3D structure
PDB1bg4 Structure of the xylanase from Penicillium simplicissimum.
ChainA
Resolution1.75 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 GOL A D68 N72 R119 Y120 K123 D68 N72 R119 Y120 K123
BS02 GOL A K193 S228 K193 S228
BS03 GOL A N48 A54 N48 A54
BS04 GOL A K51 H84 Q208 E238 W268 K51 H84 Q208 E238 W268
BS05 GOL A S5 D7 S5 D7
BS06 GOL A E47 N48 K51 Q91 E47 N48 K51 Q91
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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Cellular Component
External links
PDB RCSB:1bg4, PDBe:1bg4, PDBj:1bg4
PDBsum1bg4
PubMed9792094
UniProtP56588|XYNA_PENSI Endo-1,4-beta-xylanase

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