Structure of PDB 4xx6 Chain B

Receptor sequence
>4xx6B (length=321) Species: 670483 (Gloeophyllum trabeum ATCC 11539) [Search protein sequence]
PTSPFETLRAAAAPRYFGAALGVPHLLNFTHDPLFDVTAVLQFNGATPEN
EMKWAYIEPERNQFNFTGGDIVAAFSAANDYVLRGHNLVWYQELAPWVET
LTGEDLWNATVNHITTVMTHYKESFNIYAWDVVNEAFNDNGTYRENVWYT
QLGPDYIPNAYAVARSVNTPSKLYINDYNTEGINNKSDALLAVVQSMKAH
NLVDGVGFQCHFFVGELPPDLEQNFARFVAAGVEIAVTELDIRMNLPPSQ
ADIEQQARDYATVVNACKAQGAACVGITTWGITDLYSWIPSTYPGEGYAL
LFDDNYVPHPAFNATIQALLA
3D structure
PDB4xx6 Crystal structure of a glycosylated endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from Gloeophyllum trabeum.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E161 N202 H237 E265 D267
Catalytic site (residue number reindexed from 1) E135 N176 H211 E239 D241
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 MAN B L311 D330 L285 D304
BS02 MAN B P316 G321 P290 G295
BS03 MAN B P316 S317 P290 S291
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:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4xx6, PDBe:4xx6, PDBj:4xx6
PDBsum4xx6
PubMed
UniProtS7Q6I2

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