Structure of PDB 4yl2 Chain D

Receptor sequence
>4yl2D (length=365) Species: 1377 (Aerococcus viridans) [Search protein sequence]
YNAPSEIKYIDVVNTYDLEEEASKVVPHGGFNYIAGASGDEWTKRANDRA
WKHKLLYPRLAQDVEAPDTSTEILGHKIKAPFIMAPIAAHGLAHATKEAG
TARAVSEFGTIMSISAYSGATFEEISEGLNGGPRWFQIYMAKDDQQNRDI
LDEAKGDGATAIILTADSTVSGNRDRDVKNKFVFPFGMPIVQRYLTAEGM
SLNNIYGASKQKISPRDIEEIAAHSGLPVFVKGIQHPEDADMAIKAGASG
IWVSNHGARQLYEAPGSFDTLPAIAERVNKRVPIVFDSGVRRGEHVAKAL
ASGADVVALGRPVLFGLALGGWQGAYSVLDYFQKDLTRVMQLTGSQNVED
LKGLDLFDNPYGYEY
3D structure
PDB4yl2 Speeding up the product release: a second-sphere contribution from Tyr191 to the reactivity of l-lactate oxidase revealed in crystallographic and kinetic studies of site-directed variants.
ChainD
Resolution1.9 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) S122 Y146 T172 D174 K241 H265
Catalytic site (residue number reindexed from 1) S115 Y139 T165 D167 K232 H256
Enzyme Commision number 1.1.3.-
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 I41 P93 I94 A95 S122 Q144 Y146 T172 K241 H265 G266 R268 D296 S297 G298 R300 G319 R320 I34 P86 I87 A88 S115 Q137 Y139 T165 K232 H256 G257 R259 D287 S288 G289 R291 G310 R311
BS02 PYR D Y40 Y146 R181 L211 Y215 H265 R268 Y33 Y139 R174 L202 Y206 H256 R259
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004459 L-lactate dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:4yl2, PDBe:4yl2, PDBj:4yl2
PDBsum4yl2
PubMed26260739
UniProtQ44467|LOX_AERVM L-lactate oxidase

[Back to BioLiP]