Structure of PDB 2pmq Chain A

Receptor sequence
>2pmqA (length=367) Species: 314265 (Salipiger bermudensis HTCC2601) [Search protein sequence]
KIAEIQLFQHDLPVVNGPYRIASGDVWSLTTTIVKIIAEDGTIGWGETCP
VGPTYAEAHAGGALAALEVLASGLAGAEALPLPLHTRMDSLLCGHNYAKS
ALDIAVHDLWGKRLGVPVHELLGGALTDSVSSYYSLGVMEPDEAARQALE
KQREGYSRLQVKLGARPIEIDIEAIRKVWEAVRGTGIALAADGNRGWTTR
DALRFSRECPDIPFVMEQPCNSFEDLEAIRPLCHHALYMDEDGTSLNTVI
TAAATSLVDGFGMKVSRIGGLQHMRAFRDFCAARNLPHTCDDAWGGDIVS
AACTHIASTVLPRLMEGAWLAQPYVAEHYDAENGVRIEGGRIRVPQGPGL
GLTIDPERFGPPLFSAE
3D structure
PDB2pmq Discovery of new enzymes and metabolic pathways by using structure and genome context.
ChainA
Resolution1.72 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 S136 Q161 K163 D193 E218 D241 E242 K265 D292 D293 A294 E317 G318 A319 W320
Catalytic site (residue number reindexed from 1) Y19 S135 Q160 K162 D192 E217 D240 E241 K264 D291 D292 A293 E316 G317 A318 W319
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 A D193 E218 D241 D192 E217 D240
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
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:2pmq, PDBe:2pmq, PDBj:2pmq
PDBsum2pmq
PubMed24056934
UniProtQ0FPQ4|HPBD_SALBH 4-hydroxyproline betaine 2-epimerase (Gene Name=hpbD)

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