Structure of PDB 3rbv Chain A

Receptor sequence
>3rbvA (length=313) Species: 46161 (Actinomadura kijaniata) [Search protein sequence]
NPIRVGVIGCADIAWRRALPALEAEPLTEVTAIASRRWDRAKRFTERFGG
EPVEGYPALLERDDVDAVYVPLPAVLHAEWIDRALRAGKHVLAEKPLTTD
RPQAERLFAVARERGLLLMENFMFLHHPQHRQVADMLDEGVIGEIRSFAA
SFTIPPKGGALLDIGVYPIRAAGLFLGADLEFVGAVLRHERDRDVVVGGN
ALLTTRQGVTAQLTFGMEHAYTNNYEFRGSTGRLWMNRVFTPPATYQPVV
HIERQDHAEQFVLPAHDQFAKSIRAFAQAVLSGEHPREWSEDSLRQASLV
DAVRTGARDIYFP
3D structure
PDB3rbv Combined Structural and Functional Investigation of a C-3''-Ketoreductase Involved in the Biosynthesis of dTDP-l-Digitoxose.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K102 Y186
Catalytic site (residue number reindexed from 1) K95 Y167
Enzyme Commision number 1.1.1.384: dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase.
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 NAP A C17 A18 D19 I20 S42 R43 Y63 P78 L79 P80 L83 H84 K102 D182 Y186 C10 A11 D12 I13 S35 R36 Y56 P71 L72 P73 L76 H77 K95 D163 Y167
BS02 PO4 A H285 K290 H266 K271
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3rbv, PDBe:3rbv, PDBj:3rbv
PDBsum3rbv
PubMed21598943
UniProtB3TMR8|KIJDR_ACTKI dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase (Gene Name=KijD10)

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