Structure of PDB 6dvh Chain D

Receptor sequence
>6dvhD (length=394) Species: 1772 (Mycolicibacterium smegmatis) [Search protein sequence]
MSNWGDYENEIYGQGLVGVAPTLPMSYADWEAHAQQALPPGVLSYVAGGS
GDEHTQRANVEAFKHWGLMPRMLMAATERDLSVELWGKTWAAPMFFAPIG
VIALCAQDGHGDAASAQASARTGVPYITSTLAVSSLEDIRKHAGDTPAYF
QLYYPEDRDLAESFIRRAEEAGYDGLVITLDTWIFGWRPRDLTISNFPFL
RGLALTNYVTDPVFQKKFKAHSGVEAEGLRDNPRLAADFWHGLFGHSVTW
EDIDWVRSITKMPVILKGIQHPDDARRAVDSGVDGIYCSNHGGRQANGGL
PALDCLPEVVKASGDTPVLFDSGIRTGADVVKALAMGASAVGIGRPYAWG
AALGGSKGIEHVARSLLAEADLIMAVDGYRNLKELTIDALRPTR
3D structure
PDB6dvh Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis.
ChainD
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) Y152 D180 H290
Catalytic site (residue number reindexed from 1) Y153 D181 H291
Enzyme Commision number 1.13.12.4: lactate 2-monooxygenase.
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 FMN D P97 I98 G99 S128 Q150 Y152 K266 H290 G291 R293 D320 S321 G322 R324 R344 P98 I99 G100 S129 Q151 Y153 K267 H291 G292 R294 D321 S322 G323 R325 R345
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0050040 lactate 2-monooxygenase activity

View graph for
Molecular Function
External links
PDB RCSB:6dvh, PDBe:6dvh, PDBj:6dvh
PDBsum6dvh
PubMed30207005
UniProtP21795|LMO_MYCSM L-lactate 2-monooxygenase

[Back to BioLiP]