Structure of PDB 5olc Chain D

Receptor sequence
>5olcD (length=351) Species: 63186 (Zobellia galactanivorans) [Search protein sequence]
SKIKKIEPYVISHKLDDTRKICIVKITLDDGTYGWGEGYGPAAVIKSGID
FFTPFLLGKEAIGHEVLWQEMYRRSMDYARSGVLQAAISAIDVALWDIKG
KLLNLPVSVLLGGVKNPIIEPYATGLYLEELLVEEALLYKSQGFKATKMK
VGLGIEQDLKYIAAIRKAIGPDMRLMIDSNHAYCYKEAIELARKAEKFDI
SWFEEPVSPEDYDGYKRLRQNTTIPISGGECEYLKYGFKRLFDKDCVDIA
QPDICAAGGLTEVKKIATLAQTYNVDLVPHTWGTWIAISAAVHLVANLDL
PTMELDRTENALRDEVTLHKIKLENGHLEVPCTPGLGVDVDMDKLEHYLD
K
3D structure
PDB5olc Carrageenan catabolism is encoded by a complex regulon in marine heterotrophic bacteria.
ChainD
Resolution2.79 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K164 K166 D194 N196 E220 G245 E246 D269 H296 E329 E334
Catalytic site (residue number reindexed from 1) K148 K150 D178 N180 E204 G229 E230 D253 H280 E304 E309
Enzyme Commision number 4.2.1.6: galactonate dehydratase.
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 D194 E220 E246 H296 D178 E204 E230 H280
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008869 galactonate dehydratase activity
GO:0016829 lyase activity
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5olc, PDBe:5olc, PDBj:5olc
PDBsum5olc
PubMed29162826
UniProtG0L7B8

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