Structure of PDB 1ur2 Chain A

Receptor sequence
>1ur2A (length=351) Species: 39650 (Cellvibrio mixtus) [Search protein sequence]
TGLKSAYKDNFLIGAALNATIASGADERLNTLIAKEFNSITPENCMKWGV
LRDAQGQWNWKDADAFVAFGTKHNLHMVGHTLVWHSQIHDEVFKNADGSY
ISKAALQKKMEEHITTLAGRYKGKLAAWDVVNEAVGDDLKMRDSHWYKIM
GDDFIYNAFTLANEVDPKAHLMYNDYNIERTGKREATVEMIERLQKRGMP
IHGLGIQGHLGIDTPPIAEIEKSIIAFAKLGLRVHFTSLDVDVLPSVWEL
PVAEVSTRFEYKPERDPYTKGLPQEMQDKLAKRYEDLFKLFIKHSDKIDR
ATFWGVSDDASWLNGFPIPGRTNYPLLFDRKLQPKDAYFRLLDLKRLEHH
H
3D structure
PDB1ur2 The Mechanisms by which Family 10 Glycoside Hydrolases Bind Decorated Substrates
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E157 N198 H233 S262 D264
Catalytic site (residue number reindexed from 1) E133 N174 H209 S238 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 N201 W272 E273 N177 W248 E249
BS02 XYP A E157 W336 E133 W312
BS03 XYS A K71 H104 Q231 H233 S262 W328 W336 K47 H80 Q207 H209 S238 W304 W312
BS04 XYP A E67 N68 K71 Q111 W328 E43 N44 K47 Q87 W304
BS05 AHR A E67 N68 E43 N44
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
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Biological Process
External links
PDB RCSB:1ur2, PDBe:1ur2, PDBj:1ur2
PDBsum1ur2
PubMed14668328
UniProtO68541

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