Structure of PDB 3rc7 Chain A

Receptor sequence
>3rc7A (length=325) Species: 46161 (Actinomadura kijaniata) [Search protein sequence]
NPIRVGVIGCADIAWRRALPALEAEPLTEVTAIASRRWDRAKRFTERFGG
EPVEGYPALLERDDVDAVYVPLPAVLHAEWIDRALRAGKHVLAEKPLTTD
RPQAERLFAVARERGLLLMENFMFLHHPQHRQVADMLDEGVIGEIRSFAA
SFTIPPKPQGDIRYQADVGGGALLDIGVFPIRAAGLFLGADLEFVGAVLR
HERDRDVVVGGNALLTTRQGVTAQLTFGMEHAYTNNYEFRGSTGRLWMNR
VFTPPATYQPVVHIERQDHAEQFVLPAHDQFAKSIRAFAQAVLSGEHPRE
WSEDSLRQASLVDAVRTGARDIYFP
3D structure
PDB3rc7 Combined Structural and Functional Investigation of a C-3''-Ketoreductase Involved in the Biosynthesis of dTDP-l-Digitoxose.
ChainA
Resolution2.0 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 F186
Catalytic site (residue number reindexed from 1) K95 F179
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 G16 C17 A18 D19 I20 S42 R43 Y63 P78 L79 P80 H84 E101 K102 I169 R170 V175 D182 G9 C10 A11 D12 I13 S35 R36 Y56 P71 L72 P73 H77 E94 K95 I162 R163 V168 D175
BS02 PO4 A H285 K290 H278 K283
BS03 TLO A R23 R24 F159 I161 P162 Y240 T260 R16 R17 F152 I154 P155 Y233 T253
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3rc7, PDBe:3rc7, PDBj:3rc7
PDBsum3rc7
PubMed21598943
UniProtB3TMR8|KIJDR_ACTKI dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase (Gene Name=KijD10)

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