Structure of PDB 1w3h Chain A

Receptor sequence
>1w3hA (length=348) Species: 155077 (Cellvibrio japonicus) [Search protein sequence]
SPGLASLADFPIGVAVAASGGNADIFTSSARQNIVRAEFNQITAENIMKM
SYMYSGSNFSFTNSDRLVSWAAQNGQTVHGHTLVWHPSYQLPNWASDSNA
NFRQDFARHIDTVAAHFAGQVKSWDVVNEALFDSADDPDGRGSANGYRQS
VFYRQFGGPEYIDEAFRRARAADPTAELYYNDFNTEENGAKTTALVNLVQ
RLLNNGVPIDGVGFQMHVMNDYPSIANIRQAMQKIVALSPTLKIKITELD
VRLNNPYDGNSSNNYTNRNDCAVSCAGLDRQKARYKEIVQAYLEVVPPGR
RGGITVWGIADPDSWLYTHQNLPDWPLLFNDNLQPKPAYQGVVEALSG
3D structure
PDB1w3h The Use of Forced Protein Evolution to Investigate and Improve Stability of Family 10 Xylanases: The Production of Ca2+-Independent Stable Xylanases
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E127 N179 H215 E246 D248
Catalytic site (residue number reindexed from 1) E129 N181 H217 E248 D250
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 A N253 D256 N258 N261 N262 N255 D258 N260 N263 N264
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1w3h, PDBe:1w3h, PDBj:1w3h
PDBsum1w3h
PubMed15452124
UniProtP14768|XYNA_CELJU Endo-1,4-beta-xylanase A (Gene Name=xynA)

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