Structure of PDB 3auj Chain L

Receptor sequence
>3aujL (length=551) Species: 571 (Klebsiella oxytoca) [Search protein sequence]
MRSKRFEALAKRPVNQDGFVKEWIEEGFIAMESPNDPKPSIKIVNGAVTE
LDGKPVSDFDLIDHFIARYGINLNRAEEVMAMDSVKLANMLCDPNVKRSE
IVPLTTAMTPAKIVEVVSHMNVVEMMMAMQKMRARRTPSQQAHVTNVKDN
PVQIAADAAEGAWRGFDEQETTVAVARYAPFNAIALLVGSQVGRPGVLTQ
CSLEEATELKLGMLGHTCYAETISVYGTEPVFTDGDDTPWSKGFLASSYA
SRGLKMRFTSGSGSEVQMGYAEGKSMLYLEARCIYITKAAGVQGLQNGSV
SCIGVPSAVPSGIRAVLAENLICSSLDLECASSNDQTFTHSDMRRTARLL
MQFLPGTDFISSGYSAVPNYDNMFAGSNEDAEDFDDYNVIQRDLKVDGGL
RPVREEDVIAIRNKAARALQAVFAGMGLPPITDEEVEAATYAHGSKDMPE
RNIVEDIKFAQEIINKNRNGLEVVKALAQGGFTDVAQDMLNIQKAKLTGD
YLHTSAIIVGDGQVLSAVNDVNDYAGPATGYRLQGERWEEIKNIPGALDP
N
3D structure
PDB3auj Redesign of coenzyme B(12) dependent diol dehydratase to be resistant to the mechanism-based inactivation by glycerol and act on longer chain 1,2-diols
ChainL
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q141 H143 E170 E221 Q296 D335 S362
Catalytic site (residue number reindexed from 1) Q141 H143 E170 E221 Q296 D335 S362
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 GOL L H143 E170 T222 Q296 D335 Q336 F374 H143 E170 T222 Q296 D335 Q336 F374 Manual survey: Km=1.2+-0.2mM (22221669)
BS02 CA L Q141 E170 E221 Q296 S362 Q141 E170 E221 Q296 S362 Manual survey: Km=1.2+-0.2mM (22221669)
BS03 B12 L T172 V173 S202 E205 S224 Q267 M268 S301 M373 F374 T172 V173 S202 E205 S224 Q267 M268 S301 M373 F374 Manual survey: Km=1.2+-0.2mM (22221669)
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:3auj, PDBe:3auj, PDBj:3auj
PDBsum3auj
PubMed22221669
UniProtQ59470

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