Structure of PDB 4izg Chain B

Receptor sequence
>4izgB (length=369) Species: 318586 (Paracoccus denitrificans PD1222) [Search protein sequence]
MKIAEIHVYAHDLPVKDGPYTIASSTVWSLQTTLVKIVADSGLAGWGETC
PVGPTYAPSHALGARAALAEMAPGLIGANPLQPLVLRRRMDGLLCGHNYA
KAAIDIAAYDLMGKHYGVRVADLLGGVAAERVPSYYATGIGQPDEIARIA
AEKVAEGFPRLQIKIGGRPVEIDIETVRKVWERIRGTGTRLAVDGNRSLP
SRDALRLSRECPEIPFVLEQPCNTLEEIAAIRGRVQHGIYLDESGEDLST
VIRAAGQGLCDGFGMKLTRIGGLQQMAAFRDICEARALPHSCDDAWGGDI
IAAACTHIGATVQPRLNEGVWVAQPYIAQPYDEENGIRIAGGHIDLPKGP
GLGITPDESLFGPPVASFS
3D structure
PDB4izg Prediction and biochemical demonstration of a catabolic pathway for the osmoprotectant proline betaine.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y20 A137 Q162 K164 D194 N196 V217 E219 D242 E243 K266 D293 D294 A295 E318 G319 V320 W321
Catalytic site (residue number reindexed from 1) Y20 A137 Q162 K164 D194 N196 V217 E219 D242 E243 K266 D293 D294 A295 E318 G319 V320 W321
Enzyme Commision number 5.1.1.22: 4-hydroxyproline betaine 2-epimerase.
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 MG B D194 E219 D242 D194 E219 D242
BS02 4OP B Y56 Y135 Q162 K164 D194 D242 K266 A295 W321 Y56 Y135 Q162 K164 D194 D242 K266 A295 W321
Gene Ontology
Molecular Function
GO:0016853 isomerase activity
GO:0016854 racemase and epimerase activity
GO:0016855 racemase and epimerase activity, acting on amino acids and derivatives
GO:0036361 racemase activity, acting on amino acids and derivatives
GO:0046872 metal ion binding
Biological Process
GO:0006579 amino-acid betaine catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4izg, PDBe:4izg, PDBj:4izg
PDBsum4izg
PubMed24520058
UniProtA1B198|HPBD_PARDP 4-hydroxyproline betaine 2-epimerase (Gene Name=hpbD)

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