Structure of PDB 4c3y Chain D

Receptor sequence
>4c3yD (length=508) Species: 1833 (Rhodococcus erythropolis) [Search protein sequence]
DWTSECDVLVVGSGGGALTGAYTAAAQGLTTIVLEKTDRFGGTSAYSGAS
IWLPGTQVQERAGLPDSTENARTYLRALLGDAESERQDAYVETAPAVVAL
LEQNPNIEFEFRAFPDYYKAEGRMDTGRSINPLDLDPADIGDLAGKVRPE
LDQDRTGQDHAPGPMIGGRALIGRLLAAVQSTGKAELRTESVLTSLIVED
GRVVGAEVESGGETQRIKANRGVLMAAGGIEGNAEMREQAGTPGKAIWSM
GPFGANTGDAISAGIAVGGATALLDQAWFCPGVEQPDGSAAFMVGVRGGL
VVDSAGERYLNESLPYDQFGRAMDAHDDNGSAVPSFMIFDSREGGGLPAI
CIPNTAPAKHLEAGTWVGADTLEELAAKTGLPADALRSTVEKFNDAAKLG
VDEEFHRGEDPYDAFFCPPNGGANAALTAIENGPFYAARIVLSDLGTKGG
LVTDVNGRVLRADGSAIDGLYAAGNTSASLSGRFYPGPGVPLGTAMVFSY
RAAQDMAK
3D structure
PDB4c3y Crystal Structure and Site-Directed Mutagenesis of 3-Ketosteroid Delta1-Dehydrogenase from Rhodococcus Erythropolis Sq1 Explain its Catalytic Mechanism
ChainD
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 L445 G446 Y485
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 D G16 E37 K38 G44 T45 S46 S49 G50 S52 V194 L195 A229 G230 N258 D261 L447 N477 G491 P493 L494 G14 E35 K36 G42 T43 S44 S47 G48 S50 V192 L193 A227 G228 N256 D259 L445 N475 G489 P491 L492
BS02 ANB D S52 F116 Y318 Y487 P490 G491 S50 F114 Y316 Y485 P488 G489
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4c3y, PDBe:4c3y, PDBj:4c3y
PDBsum4c3y
PubMed24165124
UniProtQ9RA02

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