Structure of PDB 4eac Chain B

Receptor sequence
>4eacB (length=395) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SHMEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKR
KAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQWIANYQQTLRNLAQCGIR
TVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEA
DYTEEEIAQAAERFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLE
LYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRPILGLPRIV
STIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTH
LRSTMREDNPKTFHEAAHLNGDVDMYEVVKAIVEEEHRRKAEGKEDLIPM
RPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFFS
3D structure
PDB4eac Structural insights into decreased enzymatic activity induced by an insert sequence in mannonate dehydratase from Gram negative bacterium.
ChainB
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) H233 C271 H298 D351 H352 Y368
Catalytic site (residue number reindexed from 1) H235 C273 H300 D353 H354 Y370
Enzyme Commision number 4.2.1.8: mannonate 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 MN B H233 C271 H298 D351 H235 C273 H300 D353
Gene Ontology
Molecular Function
GO:0008198 ferrous iron binding
GO:0008927 mannonate dehydratase activity
GO:0016829 lyase activity
GO:0030145 manganese ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006064 glucuronate catabolic process
GO:0006974 DNA damage response
GO:0042840 D-glucuronate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4eac, PDBe:4eac, PDBj:4eac
PDBsum4eac
PubMed22796868
UniProtP24215|UXUA_ECOLI Mannonate dehydratase (Gene Name=uxuA)

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