Structure of PDB 4il2 Chain D

Receptor sequence
>4il2D (length=380) Species: 199310 (Escherichia coli CFT073) [Search protein sequence]
KIVKAEVFVTCPGRNFVTLKITTEDGITGLGDATLNGRELSVASYLQDHL
CPQLIGRDAHRIEDIWQFFYKGAYWRRGPVTMSAISAVDMALWDIKAKAA
NMPLYQLLGGASREGVMVYCHTTGHSIDEALDDYARHQELGFKAIRVQCG
IPGPEEQLWSTEKYLDFMPKLFDAVRNKFGFDEHLLHDMHHRLTPIEAAR
FGKSIEDYRMFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQ
LIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDLSPVCM
AAALHFDLWVPNFGVQEYMGYSEQMLEVFPHNWTFDNGYMHPGEKPGLGI
EFDEKLAAKYPYEPAYLPVARLEDGTLWNW
3D structure
PDB4il2 Mannonate degradation pathway in E. coli CFT073
ChainD
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L47 G49 W87 R158 Q160 D223 H225 E249 G274 E275 R296 T298 H325 E352 W415
Catalytic site (residue number reindexed from 1) L35 G37 W75 R146 Q148 D188 H190 E214 G239 E240 R261 T263 H290 E317 W380
Enzyme Commision number 4.2.1.-
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 MG D D223 D250 E275 D188 D215 E240
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008927 mannonate dehydratase activity
GO:0016829 lyase 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:4il2, PDBe:4il2, PDBj:4il2
PDBsum4il2
PubMed
UniProtQ8FHC7|MAND_ECOL6 D-galactonate dehydratase family member RspA (Gene Name=rspA)

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