Structure of PDB 4c3y Chain C

Receptor sequence
>4c3yC (length=505) Species: 1833 (Rhodococcus erythropolis) [Search protein sequence]
DWTSECDVLVVGSGGGALTGAYTAAAQGLTTIVLEKTDRFGGTSAYSGAS
IWLPGTQVQERAGLPDSTENARTYLRALLGDAESERQDAYVETAPAVVAL
LEQNPNIEFEFRAFPDYYKAEGRMDTGRSINPLDLDPADIGDLAGKVRPE
LDQDRTGQDHAPGPMIGGRALIGRLLAAVQSTGKAELRTESVLTSLIVED
GRVVGAEVESGGETQRIKANRGVLMAAGGIEGNAEMREQAGTPGKAIWSM
GPFGANTGDAISAGIAVGGATALLDQAWFCPGVEQPDGSAAFMVGVRGGL
VVDSAGERYLNESLPYDQFGRAMDAHDDNGSAVPSFMIFDSREGGGLPAI
CIPNTAPAKHLEAGTWVGADTLEELAAKTGLPADALRSTVEKFNDAAKLG
VDEEFHRGEDPYDAFFCPGANAALTAIENGPFYAARIVLSDLGTKGGLVT
DVNGRVLRADGSAIDGLYAAGNTSASLSGRFYPGPGVPLGTAMVFSYRAA
QDMAK
3D structure
PDB4c3y Crystal Structure and Site-Directed Mutagenesis of 3-Ketosteroid Delta1-Dehydrogenase from Rhodococcus Erythropolis Sq1 Explain its Catalytic Mechanism
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C282 V296 R299 Y318 L447 G448 Y487
Catalytic site (residue number reindexed from 1) C280 V294 R297 Y316 L442 G443 Y482
Enzyme Commision number 1.3.99.4: 3-oxosteroid 1-dehydrogenase.
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 FAD C V13 G16 L36 E37 K38 G44 T45 S46 S49 G50 S52 L195 A229 G230 A257 N258 D261 L447 N477 G491 P493 L494 V11 G14 L34 E35 K36 G42 T43 S44 S47 G48 S50 L193 A227 G228 A255 N256 D259 L442 N472 G486 P488 L489
BS02 ANB C S52 F116 Y318 Y487 P490 S50 F114 Y316 Y482 P485
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0033765 steroid dehydrogenase activity, acting on the CH-CH group of donors
GO:0047571 3-oxosteroid 1-dehydrogenase activity
Biological Process
GO:0008202 steroid metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4c3y, PDBe:4c3y, PDBj:4c3y
PDBsum4c3y
PubMed24165124
UniProtQ9RA02

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