Structure of PDB 1iwb Chain L

Receptor sequence
>1iwbL (length=551) Species: 571 (Klebsiella oxytoca) [Search protein sequence]
MRSKRFEALAKRPVNQDGFVKEWIEEGFIAMESPNDPKPSIKIVNGAVTE
LDGKPVSDFDLIDHFIARYGINLNRAEEVMAMDSVKLANMLCDPNVKRSE
IVPLTTAMTPAKIVEVVSHMNVVEMMMAMQKMRARRTPSQQAHVTNVKDN
PVQIAADAAEGAWRGFDEQETTVAVARYAPFNAIALLVGSQVGRPGVLTQ
CSLEEATELKLGMLGHTCYAETISVYGTEPVFTDGDDTPWSKGFLASSYA
SRGLKMRFTSGSGSEVQMGYAEGKSMLYLEARCIYITKAAGVQGLQNGSV
SCIGVPSAVPSGIRAVLAENLICSSLDLECASSNDQTFTHSDMRRTARLL
MQFLPGTDFISSGYSAVPNYDNMFAGSNEDAEDFDDYNVIQRDLKVDGGL
RPVREEDVIAIRNKAARALQAVFAGMGLPPITDEEVEAATYAHGSKDMPE
RNIVEDIKFAQEIINKNRNGLEVVKALAQGGFTDVAQDMLNIQKAKLTGD
YLHTSAIIVGDGQVLSAVNDVNDYAGPATGYRLQGERWEEIKNIPGALDP
N
3D structure
PDB1iwb Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase
ChainL
Resolution1.85 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 K L Q141 H143 E170 E221 Q296 S362 G363 Q141 H143 E170 E221 Q296 S362 G363
BS02 K L S260 G261 S262 S264 E265 E280 C283 S260 G261 S262 S264 E265 E280 C283
BS03 K L S202 L203 E204 E205 E208 T222 I223 S202 L203 E204 E205 E208 T222 I223
BS04 B12 L E205 Q267 M268 S301 F374 E205 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:1iwb, PDBe:1iwb, PDBj:1iwb
PDBsum1iwb
PubMed12379103
UniProtQ59470

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