Structure of PDB 1kbj Chain A

Receptor sequence
>1kbjA (length=393) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GETKEDIARKEQLKSLLPPLDNIINLYDFEYLASQTLTKQAWAYYSSGAN
DEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATAL
CKLGNPLEGEKDVARGCGQGVTKVPQMISTLASCSPEEIIEAAPSDKQIQ
WYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREKDMKLKFSA
SRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGVSGV
VLSNHGGRQLDFSRAPIEVLAETMPILEQRNLKDKLEVFVDGGVRRGTDV
LKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVT
SIAELKPDLLDLSTLKARTVGVPNDVLYNEVYEGPTLTEFEDA
3D structure
PDB1kbj Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S228 Y254 T280 D282 K349 H373
Catalytic site (residue number reindexed from 1) S129 Y155 T181 D183 K231 H255
Enzyme Commision number 1.1.2.3: L-lactate dehydrogenase (cytochrome).
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 A Y144 S195 A196 T197 A198 S228 Q252 Y254 T280 K349 H373 R376 D409 G410 R413 G432 R433 Y45 S96 A97 T98 A99 S129 Q153 Y155 T181 K231 H255 R258 D291 G292 R295 G314 R315
Gene Ontology
Molecular Function
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:1kbj, PDBe:1kbj, PDBj:1kbj
PDBsum1kbj
PubMed11914072
UniProtP00175|CYB2_YEAST L-lactate dehydrogenase (cytochrome) (Gene Name=CYB2)

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