Structure of PDB 3ck5 Chain B

Receptor sequence
>3ck5B (length=357) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence]
LIERVRTDLYRIPLPTRLTDSTHGAMMDFELITVRIEDSDGATGLGYTYT
VNHGGAAVATMVDKDLRGCLLGADAEQIEKIWQSMWWRLHYAGRGGHATS
AISAVDIALWDLKGIRARTPLWKLFGGYDPVVPVYAGGIDLELPVADLKT
QADRFLAGGFRAIKMKVGRPDLKEDVDRVSALREHLGDSFPLMVDANMKW
TVDGAIRAARALAPFDLHWIEEPTIPDDLVGNARIVRESGHTIAGGENLH
TLYDFHNAVRAGSLTLPEPDVSNIGGYTTFRKVAALAEANNMLLTSHGVH
DLTVHALASVPHRTYMEAHLHAYMAEPMAVTDGCVSAPDRPGHGVVLDFE
RLGRLAV
3D structure
PDB3ck5 Crystal structure of a racemase from Streptomyces coelicolor A3(2) with bound magnesium.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T21 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) T19 T50 G137 K164 K166 D195 N197 I220 E221 I243 G246 E247 E268 D270 H297 G298 V299 Y315 E317
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 B D197 E223 E249 D195 E221 E247
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

View graph for
Molecular Function
View graph for
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)

[Back to BioLiP]