Structure of PDB 5ysr Chain C

Receptor sequence
>5ysrC (length=453) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQV
LSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYV
LSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTT
IGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVE
NLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICG
SEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANF
GADQVTMEARNYGLARHYDPFIVNTVVGFIGPEYLYNDRQIIRAGLEDHF
MGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDI
MLNYQTTAFHDTATVRQLLNLRPSPEFERWLESMGIMANGRLTKRAGDPS
LFF
3D structure
PDB5ysr Direct Participation of a Peripheral Side Chain of a Corrin Ring in Coenzyme B12Catalysis.
ChainC
Resolution2.05 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 B12 C V195 T196 A226 H227 Q246 S247 F258 F329 I330 M401 L402 V195 T196 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:5ysr, PDBe:5ysr, PDBj:5ysr
PDBsum5ysr
PubMed29797764
UniProtP0AEJ6|EUTB_ECOLI Ethanolamine ammonia-lyase large subunit (Gene Name=eutB)

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