Structure of PDB 3g0i Chain A

Receptor sequence
>3g0iA (length=385) Species: 5061 (Aspergillus niger) [Search protein sequence]
KAFAKFPSSASISPNPFTVSIPDEQLDDLKTLVRLSKIAPPTYESLQADG
RFGITSEWLTTMREKWLSEFDWRPFEARLNSFPQFTTEIEGLTIHFAALF
SEREDAVPIALLHGWPGSFVEFYPILQLFREEYTPETLPFHLVVPSLPGY
TFSSGPPLDKDFGLMDNARVVDQLMKDLGFGSGYIIQGGDIGSFVGRLLG
VGFDACKAVHLNLCAMRAPPEGPSIESLSAAEKEGIARMEKFMTDGLAYA
MEHSTRPSTIGHVLSSSPIALLAWIGEKYLQWVDKPLPSETILEMVSLYW
LTESFPRAIHTYRETTPMLQKELYIHKPFGFSFFPKDLCPVPRSWIATTG
NLVFFRDHAEGGHFAALERPRELKTDLTAFVEQVW
3D structure
PDB3g0i Directed evolution of an enantioselective epoxide hydrolase: uncovering the source of enantioselectivity at each evolutionary stage
ChainA
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.3.2.3: Transferred entry: 3.3.2.9 and 3.3.2.10.
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 VPR A D192 L215 F244 Y251 Y314 T317 D190 L213 F242 Y249 Y312 T315 PDBbind-CN: -logKd/Ki=3.60,Ki=250uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004301 epoxide hydrolase activity
GO:0016787 hydrolase activity
GO:0016803 ether hydrolase activity
Biological Process
GO:0097176 epoxide metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3g0i, PDBe:3g0i, PDBj:3g0i
PDBsum3g0i
PubMed19469578
UniProtQ9UR30

[Back to BioLiP]