Structure of PDB 1clx Chain C

Receptor sequence
>1clxC (length=345) Species: 155077 (Cellvibrio japonicus) [Search protein sequence]
GLASLADFPIGVAVAASGGNADIFTSSARQNIVRAEFNQITAENIMKMSY
MYSGSNFSFTNSDRLVSWAAQNGQTVHGHALVWHPSYQLPNWASDSNANF
RQDFARHIDTVAAHFAGQVKSWDVVNEALFDSADDPDGRGSANGYRQSVF
YRQFGGPEYIDEAFRRARAADPTAELYYNDFNTEENGAKTTALVNLVQRL
LNNGVPIDGVGFQMHVMNDYPSIANIRQAMQKIVALSPTLKIKITELDVR
LNNPYDGNSSNDYTNRNDCAVSCAGLDRQKARYKEIVQAYLEVVPPGRRG
GITVWGIADPDSWLYTHQNLPDWPLLFNDNLQPKPAYQGVVEALS
3D structure
PDB1clx Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution.
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E127 N179 H215 E246 D248
Catalytic site (residue number reindexed from 1) E127 N179 H215 E246 D248
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 CA C N253 D256 N258 N261 D262 N253 D256 N258 N261 D262
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1clx, PDBe:1clx, PDBj:1clx
PDBsum1clx
PubMed15299710
UniProtP14768|XYNA_CELJU Endo-1,4-beta-xylanase A (Gene Name=xynA)

[Back to BioLiP]