Structure of PDB 6qkg Chain B

Receptor sequence
>6qkgB (length=664) Species: 700510 (bacterium enrichment culture clone N47) [Search protein sequence]
MYENLCKPIKIGNHLVKNRMKYAATVDNFCDTKNGNVIDREIEYLRERAK
GGFGIVVSQGGYTHILGKGYVGQMGLVEESHLPGLKKLADAINAEGAMSI
GQIMHTGRYGHAHEYGIHEAIAGGKTVGPEPVGPTAMSSPIKRYSPCREM
TPEEIEEQIQAHIVAARMFKQTGWKGVEVCAIVGYLIADFLSRWTNKRTD
KWGGSLENRARFLIEILKGIRKEVGDDYPLVMRLNSTDLIEGGNTDEEYI
EIAKMCEAAVRIDLFSITVGWHESPGAAITAEKRPGDWLHLADNWKKAGI
KAPICMAYRMNQPDVAEKAVAEGRIDIWEMCRPGIADPYLPKKVCEGRPE
DIVTCTACNQGCFYYVFIDAIMGCMVNPRVGNEWDPAYAINPAAKKKKVL
VVGAGPSGMECARLAAVRGHDVTIMEKSDSIGGEVKLGVKSPLLYDWAET
IRYYKAQIDKLGIKLKLNTEATADSIKAEAPDVLVIATGGKPSRPKIEGI
DNKIVTNVFDILEGKVKLGDKVVFIGGNEISIQTAEYVAEQGKEVTVLEK
GKHICFDVNIFNILQHRRLMAKLNMKSMTNVTINEINDDGVEISTAGGKD
VTIEADNVVVAEGMDADDALAKAVGTKIAPEVYSIGDCAGVRKLYEAIHD
GYKMGVKIRGSLEV
3D structure
PDB6qkg Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V38 C192 V195 Y197 R245 E253 H284 Q372
Catalytic site (residue number reindexed from 1) V26 C180 V183 Y185 R233 E241 H272 Q360
Enzyme Commision number ?
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6qkg, PDBe:6qkg, PDBj:6qkg
PDBsum6qkg
PubMed31061390
UniProtE1YD54

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