Structure of PDB 4c3y Chain B

Receptor sequence

>4c3yB (length=505) Species: 1833 (Rhodococcus erythropolis)

DWTSECDVLVVGSGGGALTGAYTAAAQGLTTIVLEKTDRFGGTSAYSGAS
IWLPGTQVQERAGLPDSTENARTYLRALLGDAESERQDAYVETAPAVVAL
LEQNPNIEFEFRAFPDYYKAEGRMDTGRSINPLDLDPADIGDLAGKVRPE
LDQDRTGQDHAPGPMIGGRALIGRLLAAVQSTGKAELRTESVLTSLIVED
GRVVGAEVESGGETQRIKANRGVLMAAGGIEGNAEMREQAGTPGKAIWSM
GPFGANTGDAISAGIAVGGATALLDQAWFCPGVEQPDGSAAFMVGVRGGL
VVDSAGERYLNESLPYDQFGRAMDAHDDNGSAVPSFMIFDSREGGGLPAI
CIPNTAPAKHLEAGTWVGADTLEELAAKTGLPADALRSTVEKFNDAAKLG
VDEEFHRGEDPYDAFFCPGANAALTAIENGPFYAARIVLSDLGTKGGLVT
DVNGRVLRADGSAIDGLYAAGNTSASLSGRFYPGPGVPLGTAMVFSYRAA
QDMAK

3D structure

• PDB: 4c3y Crystal Structure and Site-Directed Mutagenesis of 3-Ketosteroid Delta1-Dehydrogenase from Rhodococcus Erythropolis Sq1 Explain its Catalytic Mechanism
• Chain: B
• Resolution: 2.3 Å

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	B	V13 G14 L36 E37 K38 G44 T45 S46 S49 G50 S52 V194 L195 A229 G230 A257 N258 D261 L447 N477 G491 P493 L494	V11 G12 L34 E35 K36 G42 T43 S44 S47 G48 S50 V192 L193 A227 G228 A255 N256 D259 L442 N472 G486 P488 L489
BS02	ANB	B	S52 F116 Y318 Y487 P490 G491	S50 F114 Y316 Y482 P485 G486

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

External links

• PDB: RCSB:4c3y, PDBe:4c3y, PDBj:4c3y
• PDBsum: 4c3y
• PubMed: 24165124
• UniProt: Q9RA02