Structure of PDB 3ovg Chain B

Receptor sequence
>3ovgB (length=351) Species: 262723 (Mycoplasmopsis synoviae 53) [Search protein sequence]
NKFARTVLGDIPVEKLGITDCHDHFIKNGGPEVEEHIDFLMLNVDASIKE
FKEFIDRGGSTIVTMDPPNVGRDVLKTLEIANAVKNLGGNVIMSTGFHKA
KFYDKYSSWLAVVPTEEIVKMCVAEIEEGMDEYNYNGPVVKRSKAKAGII
KAGTGYGAIDRLELKALEVAARTSILTGCPILVHTQLGTMALEVAKHLIG
FGANPDKIQISHLNKNPDKYYYEKVIKETGVTLCFDGPDRVKYYPDSLLA
ENIKYLVDKGLQKHITLSLDAGRILYQRNYGLTKGKQTFGLAYLFDRFLP
LLKQVGVSKEAIFDILVNNPKRVLAFDEKRNFDPLKVSKEVLELKKELNL
N
3D structure
PDB3ovg The crystal structure of an amidohydrolase from Mycoplasma synoviae with Zn ion bound
ChainB
Resolution2.059 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H24 H26 K153 H186 H214 K217 G239 D272
Catalytic site (residue number reindexed from 1) H22 H24 K151 H184 H212 K215 G237 D270
Enzyme Commision number 3.1.1.104: 5-phospho-D-xylono-1,4-lactonase.
3.1.1.25: 1,4-lactonase.
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 ZN B K153 H186 H214 K151 H184 H212
BS02 ZN B H24 H26 K153 D272 H22 H24 K151 D270
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0050490 1,4-lactonase activity
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ovg, PDBe:3ovg, PDBj:3ovg
PDBsum3ovg
PubMed
UniProtQ4A724|PFLAC_MYCS5 Phospho-furanose lactonase (Gene Name=MS53_0025)

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