Structure of PDB 2jjb Chain C

Receptor sequence
>2jjbC (length=500) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMILADYRMQQNQSG
FDLRHFVNVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRSTENTEKWD
SLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHE
IDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKE
YAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIAT
AKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDL
NSLMFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQGWY
ADYDLKSHKVRNQLTAAALFPLYVNAAAKDRANKMATATKTHLLQPGGLN
TTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQHT
YDREKKLVEKYDVSTTYPLQDGFGWTNGVTLKMLDLICPKEQPCDNVPAT
3D structure
PDB2jjb Total Syntheses of Casuarine and its 6-O-Alpha-Glucoside: Complementary Inhibition Towards Glycoside Hydrolases of the Gh31 and Gh37 Families.
ChainC
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.28: alpha,alpha-trehalase.
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 3CU C F153 W159 D160 G310 D312 W447 F518 W520 F116 W122 D123 G273 D275 W410 F473 W475
BS02 GLC C R152 Y157 N196 Y202 R205 R277 E279 D312 R115 Y120 N159 Y165 R168 R240 E242 D275
Gene Ontology
Molecular Function
GO:0004555 alpha,alpha-trehalase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005991 trehalose metabolic process
GO:0005993 trehalose catabolic process
GO:0006974 DNA damage response
GO:0071474 cellular hyperosmotic response
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2jjb, PDBe:2jjb, PDBj:2jjb
PDBsum2jjb
PubMed19123216
UniProtP13482|TREA_ECOLI Periplasmic trehalase (Gene Name=treA)

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