Structure of PDB 1iwb Chain A

Receptor sequence

>1iwbA (length=551) Species: 571 (Klebsiella oxytoca)

MRSKRFEALAKRPVNQDGFVKEWIEEGFIAMESPNDPKPSIKIVNGAVTE
LDGKPVSDFDLIDHFIARYGINLNRAEEVMAMDSVKLANMLCDPNVKRSE
IVPLTTAMTPAKIVEVVSHMNVVEMMMAMQKMRARRTPSQQAHVTNVKDN
PVQIAADAAEGAWRGFDEQETTVAVARYAPFNAIALLVGSQVGRPGVLTQ
CSLEEATELKLGMLGHTCYAETISVYGTEPVFTDGDDTPWSKGFLASSYA
SRGLKMRFTSGSGSEVQMGYAEGKSMLYLEARCIYITKAAGVQGLQNGSV
SCIGVPSAVPSGIRAVLAENLICSSLDLECASSNDQTFTHSDMRRTARLL
MQFLPGTDFISSGYSAVPNYDNMFAGSNEDAEDFDDYNVIQRDLKVDGGL
RPVREEDVIAIRNKAARALQAVFAGMGLPPITDEEVEAATYAHGSKDMPE
RNIVEDIKFAQEIINKNRNGLEVVKALAQGGFTDVAQDMLNIQKAKLTGD
YLHTSAIIVGDGQVLSAVNDVNDYAGPATGYRLQGERWEEIKNIPGALDP
N

3D structure

• PDB: 1iwb Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase
• Chain: A
• Resolution: 1.85 Å

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	A	Q141 H143 E170 E221 Q296 S362 G363	Q141 H143 E170 E221 Q296 S362 G363
BS02	K	A	S260 G261 S262 S264 E265 L279 E280 C283	S260 G261 S262 S264 E265 L279 E280 C283
BS03	K	A	L203 E204 E205 E208 T222 I223	L203 E204 E205 E208 T222 I223
BS04	B12	A	T172 Q267 M268 S301 M373 F374	T172 Q267 M268 S301 M373 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

External links

• PDB: RCSB:1iwb, PDBe:1iwb, PDBj:1iwb
• PDBsum: 1iwb
• PubMed: 12379103
• UniProt: Q59470