Structure of PDB 3ck5 Chain D

Receptor sequence
>3ck5D (length=334) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence]
LIERVRTDLYRIPLDFELITVRIEDSDGATGLGYTYTVNHGGAAVATMVD
KDLRGCLLGADAEQIEKIWQSMWWRLHYAGRGGHATSAISAVDIALWDLK
GIRARTPLWKLFGGYDPVVPVYAGGIDLELPVADLKTQADRFLAGGFRAI
KMKVGRPDLKEDVDRVSALREHLGDSFPLMVDANMKWTVDGAIRAARALA
PFDLHWIEEPTIPDDLVGNARIVRESGHTIAGGENLHTLYDFHNAVRAGS
LTLPEPDVSNIGGYTTFRKVAALAEANNMLLTSHGVHDLTVHALASVPHR
TYMEAHMAVTDGCVSAPDRPGHGVVLDFERLGRL
3D structure
PDB3ck5 Crystal structure of a racemase from Streptomyces coelicolor A3(2) with bound magnesium.
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T52 G139 K166 K168 D197 N199 I222 E223 I245 G248 E249 E270 D272 H299 G300 V301 Y317 E319
Catalytic site (residue number reindexed from 1) T37 G124 K151 K153 D182 N184 I207 E208 I230 G233 E234 E255 D257 H284 G285 V286 Y302 E304
Enzyme Commision number 5.5.1.25: 3,6-anhydro-L-galactonate cycloisomerase.
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 MG D D197 E223 E249 D182 E208 E234
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process
GO:0019388 galactose catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ck5, PDBe:3ck5, PDBj:3ck5
PDBsum3ck5
PubMed
UniProtQ9RKF7|ACI_STRCO 3,6-anhydro-alpha-L-galactonate cycloisomerase (Gene Name=SCO3480)

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