Structure of PDB 4l4p Chain A

Receptor sequence
>4l4pA (length=328) Species: 521460 (Caldicellulosiruptor bescii DSM 6725) [Search protein sequence]
TVSLTEKYKEFFKIGAAVTVKDFEGIHGRILTKHFNSLTPENDMKFERIH
PKEDFYNFEATDKIKDFALKHNMQLRGHTLVWHNQTPEWVFRDNDKEAPK
ELVIERLREHIKTICTRYRDVVYSWDVVNAAVEDKTDVLLRDSKWRRIIG
DDYIKIAFEIAKKYTGNGKLFYNDYNNEMPYKLEKTYKVLKSLLEEGTPI
DGVGIQAHWNIWDKNLIDNLKRAIETYASLGLEIQITELDISVFEFEDRR
TDLLEPTEEMVELQAKVYEDVFRVFREYRDVITSVTLWGISDRHTWKDNF
PVIGRKDWPLLFDIDGKPKKAFFRIIDF
3D structure
PDB4l4p Crystal structure of CbXyn10B from Caldicellulosiruptor bescii and its mutant(E139A) in complex with xylotriose
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A139 N182 H217 E247 D249
Catalytic site (residue number reindexed from 1) A130 N173 H208 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 K54 H87 W91 N138 Q215 E247 W305 K45 H78 W82 N129 Q206 E238 W296
BS02 XYP A E50 N51 K54 Q94 W297 W305 E41 N42 K45 Q85 W288 W296
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4l4p, PDBe:4l4p, PDBj:4l4p
PDBsum4l4p
PubMed
UniProtB9MMA5

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