Structure of PDB 1b3z Chain A

Receptor sequence

>1b3zA (length=302) Species: 69488 (Penicillium simplicissimum)

QASVSIDAKFKAHGKKYLGTIGDQYTLTKNTKNPAIIKADFGQLTPENSM
KWDATEPNRGQFTFSGSDYLVNFAQSNGKLIRGHTLVWHSQLPGWVSSIT
DKNTLISVLKNHITTVMTRYKGKIYAWDVLNEIFNEDGSLRNSVFYNVIG
EDYVRIAFETARSVDPNAKLYINDYNLDSAGYSKVNGMVSHVKKWLAAGI
PIDGIGSQTHLGAGAGSAVAGALNALASAGTKEIAITELDIAGASSTDYV
NVVNACLNQAKCVGITVWGVADPDSWRSSSSPLLFDGNYNPKAAYNAIAN
AL

3D structure

• PDB: 1b3z Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant.
• Chain: A
• Resolution: 2.3 Å

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 W88 E132 E238 W268 W276	K51 H84 W88 E132 E238 W268 W276
BS02	XYP	A	E47 N48 K51 Q91	E47 N48 K51 Q91
BS03	XYP	A	E132 Y175 W276	E132 Y175 W276
BS04	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

External links

• PDB: RCSB:1b3z, PDBe:1b3z, PDBj:1b3z
• PDBsum: 1b3z
• PubMed: 10029534
• UniProt: P56588|XYNA_PENSI Endo-1,4-beta-xylanase