Structure of PDB 3abo Chain A

Receptor sequence
>3aboA (length=453) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQV
LSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYV
LSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTT
IGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVE
NLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICG
SEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANF
GADQVTMEARNYGLARHYDPFIVNTVVGFIGPEYLYNDRQIIRAGLEDHF
MGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDI
MLNYQTTAFHDTATVRQLLNLRPSPEFERWLESMGIMANGRLTKRAGDPS
LFF
3D structure
PDB3abo Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.3.1.7: ethanolamine ammonia-lyase.
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 ETA A R160 Q162 N193 E287 D362 Y404 R160 Q162 N193 E287 D362 Y404
BS02 B12 A P194 A226 H227 Q246 S247 F258 F329 I330 M401 L402 P194 A226 H227 Q246 S247 F258 F329 I330 M401 L402
Gene Ontology
Molecular Function
GO:0008851 ethanolamine ammonia-lyase activity
GO:0016829 lyase activity
GO:0031419 cobalamin binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0046336 ethanolamine catabolic process
Cellular Component
GO:0005829 cytosol
GO:0009350 ethanolamine ammonia-lyase complex
GO:0031469 bacterial microcompartment
GO:0031471 ethanolamine degradation polyhedral organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3abo, PDBe:3abo, PDBj:3abo
PDBsum3abo
PubMed20519496
UniProtP0AEJ6|EUTB_ECOLI Ethanolamine ammonia-lyase large subunit (Gene Name=eutB)

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