Structure of PDB 4o08 Chain B

Receptor sequence
>4o08B (length=284) Species: 1404 (Priestia megaterium) [Search protein sequence]
QYINVNGVNLHYISKGQGELMLFLHGFPDFSHIWRHQIDEFSNDFHTVAL
DLRGYNLSEKPSGLESYEIDVLVEDIRQVIEGLGYSSCTLVVHDWGAGIG
WTFAYRYPEYVQKLIAFNGPHPYTFMRELRTNKNQQKASEYMKWFQKQEV
QDYMERDNFSGLRKLVIDPGVKKGYLTADDVQAYMNSWENGSVLSMLSYY
RNLKIFTEEDLRRKSLFPLEEEVLNIPVQIIWGNQDPTFMPENLDGIEEY
VPNISVHRLAEASHAPQHEKPQEVNNVMWNFLNK
3D structure
PDB4o08 Engineering of an epoxide hydrolase for efficient bioresolution of bulky pharmaco substrates.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F30 D97 W98 N121 L132 Y144 Y203 D239 H267
Catalytic site (residue number reindexed from 1) F27 D94 W95 N118 L129 Y141 Y200 D236 H264
Enzyme Commision number 3.2.2.10: pyrimidine-5'-nucleotide nucleosidase.
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 PO6 B F30 L168 V169 P240 H267 F27 L165 V166 P237 H264
BS02 PO6 B D97 W98 P123 Y144 M145 Y203 D94 W95 P120 Y141 M142 Y200
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0047405 pyrimidine-5'-nucleotide nucleosidase activity

View graph for
Molecular Function
External links
PDB RCSB:4o08, PDBe:4o08, PDBj:4o08
PDBsum4o08
PubMed25331869
UniProtG9BEX6

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