Structure of PDB 5ysh Chain G

Receptor sequence
>5yshG (length=550) Species: 571 (Klebsiella oxytoca) [Search protein sequence]
MRSKRFEALAKRPVNQDGFVKEWIEEGFIAMESPNDPKPSIKIVNGAVTE
LDGKPVSDFDLIDHFIARYGINLNRAEEVMAMDSVKLANMLCDPNVKRSE
IVPLTTAMTPAKIVEVVSHMNVVEMMMAMQKMRARRTPSQQAHVTNVKDN
PVQIAADAAEGAWRGFDEQETAVAVARYAPFNAIALLVGSQVGRPGVLTQ
CSLEEATELKLGMLGHTCYAETISVYGTEPVFTDGDDTPWSKGFLASSYA
SRGLKMRFTSGSGSEVQMGYAEGKSMLYLEARCIYITKAAGVQGLQNGSV
SCIGVPSAVPSGIRAVLAENLICSSLDLECASSNDQTFTHSDMRRTARLL
MQFLPGTDFISSGYSAVPNYDNMFAGSNEDAEDFDDYNVIQRDLKVDGGL
RPVREEDVIAIRNKAARALQAVFAGMGLPPITDEEVEAATYAHGSKDMPE
RNIVEDIKFAQEIINKNRNGLEVVKALAQGGFTDVAQDMLNIQKAKLTGD
YLHTSAIIVGDGQVLSAVNDVNDYAGPATGYRLQGERWEEIKNIPGALDP
3D structure
PDB5ysh Direct Participation of a Peripheral Side Chain of a Corrin Ring in Coenzyme B12Catalysis.
ChainG
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.1.28: propanediol 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 CA G Q141 E170 E221 Q296 S362 Q141 E170 E221 Q296 S362
BS02 B12 G E205 D234 Q267 M268 S301 F374 E205 D234 Q267 M268 S301 F374
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
GO:0050215 propanediol dehydratase activity

View graph for
Molecular Function
External links
PDB RCSB:5ysh, PDBe:5ysh, PDBj:5ysh
PDBsum5ysh
PubMed29797764
UniProtQ59470

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