Structure of PDB 3ktc Chain B

Receptor sequence
>3ktcB (length=330) Species: 218491 (Pectobacterium atrosepticum SCRI1043) [Search protein sequence]
ATYNYPEFGAGLWHFANYIDRYAVDGYGPALSTIDQINAAKEVGELSYVD
LPYPFTPGVTLSEVKDALKDAGLKAIGITPEIYLQKWSRGAFTNPDPAAR
AAAFELMHESAGIVRELGANYVKVWPGQDGWDYPFQVSHKNLWKLAVDGM
RDLAGANPDVKFAIEYKPREPRVKMTWDSAARTLLGIEDIGLDNVGVLLD
FGHALYGGESPADSAQLIIDRGRLFGMDVNDNLRGWDDDLVVGTVHMTEI
FEFFYVLKINNWQGVWQLDQFPFRENHVEAAQLSIRFLKHIYRALDKLDI
PALQAAQEAQNPLQAQRIVQDALLSSITVS
3D structure
PDB3ktc Crystal structure of Putative sugar isomerase (YP_050048.1) from ERWINIA CAROTOVORA ATROSEPTICA SCRI1043 at 1.54 A resolution
ChainB
Resolution1.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E166 K168 D201 H204 D229 D238 D240
Catalytic site (residue number reindexed from 1) E165 K167 D200 H203 D228 D237 D239
Enzyme Commision number 5.3.1.36: D-apiose isomerase.
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 FE B K168 H204 D238 D240 K167 H203 D237 D239
BS02 FE B E166 D201 D229 D270 E165 D200 D228 D269
Gene Ontology
Molecular Function
GO:0008740 L-rhamnose isomerase activity
GO:0009045 xylose isomerase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0019301 rhamnose catabolic process
GO:0019324 L-lyxose metabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3ktc, PDBe:3ktc, PDBj:3ktc
PDBsum3ktc
PubMed
UniProtQ6D5T7|APSI_PECAS D-apiose isomerase (Gene Name=apsI)

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