Structure of PDB 5xd8 Chain A

Receptor sequence
>5xd8A (length=352) Species: 1116375 (Vibrio sp. EJY3) [Search protein sequence]
MKTTIKDIKTRLFKIPLKDHFELITTTVTLEDGSQGTGYTYTGGKGGYSI
KAMLEYDIQPALIGKDATQIEEIYDFMEWHIHYVGRGGISTFAMSAVDIA
LWDLKGKREGLPLWKMAGGKNNTCKAYCGGIDLQFPLEKLLNNICGYLES
GFNAVKIKIGRENMQEDIDRIKAVRELIGPDITFMIDANYSLTVEQAIKL
SKAVEQYDITWFEEPTLPDDYKGFAEIADNTAIPLAMGENLHTIHEFGYA
MDQAKLGYCQPDASNCGGITGWLKAADLITEHNIPVCTHGMQELHVSLVS
AFDTGWLEVHSFPIDEYTKRPLVVENFRAVASNEPGIGVEFDWDKIAQYE
VH
3D structure
PDB5xd8 Crystal structure analysis of 3,6-anhydro-l-galactonate cycloisomerase suggests emergence of novel substrate specificity in the enolase superfamily
ChainA
Resolution2.505 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T53 G140 K167 K169 D198 N200 E224 G249 E250 Q271 D273 H300 G301 M302 W317 E319 P324
Catalytic site (residue number reindexed from 1) T42 G129 K156 K158 D187 N189 E213 G238 E239 Q260 D262 H289 G290 M291 W306 E308 P313
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 A D198 E224 E250 D187 E213 E239
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: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:5xd8, PDBe:5xd8, PDBj:5xd8
PDBsum5xd8
PubMed28716734
UniProtH2IFX0|ACI_VIBSJ 3,6-anhydro-alpha-L-galactonate cycloisomerase (Gene Name=Vejaci)

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