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3K9Y

Crystal structure of rat mitochondrial P450 24A1 S57D in complex with CYMAL-5

Functional Information from GO Data
ChainGOidnamespacecontents
A0001649biological_processosteoblast differentiation
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005739cellular_componentmitochondrion
A0006629biological_processlipid metabolic process
A0008202biological_processsteroid metabolic process
A0008403molecular_function25-hydroxycholecalciferol-24-hydroxylase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0030342molecular_function1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity
A0033280biological_processresponse to vitamin D
A0042359biological_processvitamin D metabolic process
A0042369biological_processvitamin D catabolic process
A0046872molecular_functionmetal ion binding
A0062180molecular_function25-hydroxycholecalciferol-23-hydroxylase activity
A0062181molecular_function1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity
A0070576molecular_functionvitamin D 24-hydroxylase activity
A0070643molecular_functionvitamin D 25-hydroxylase activity
A0071305biological_processcellular response to vitamin D
B0001649biological_processosteoblast differentiation
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005739cellular_componentmitochondrion
B0006629biological_processlipid metabolic process
B0008202biological_processsteroid metabolic process
B0008403molecular_function25-hydroxycholecalciferol-24-hydroxylase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0030342molecular_function1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity
B0033280biological_processresponse to vitamin D
B0042359biological_processvitamin D metabolic process
B0042369biological_processvitamin D catabolic process
B0046872molecular_functionmetal ion binding
B0062180molecular_function25-hydroxycholecalciferol-23-hydroxylase activity
B0062181molecular_function1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity
B0070576molecular_functionvitamin D 24-hydroxylase activity
B0070643molecular_functionvitamin D 25-hydroxylase activity
B0071305biological_processcellular response to vitamin D
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CM5 A 516
ChainResidue
AMET246
ASER247
APHE249
ACM5517

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CM5 A 517
ChainResidue
AGLN82
APHE393
AHIS497
ACM5516
BLEU66

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGiGKRMCIG
ChainResidueDetails
APHE455-GLY464

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0007744|PDB:3K9V, ECO:0007744|PDB:3K9Y
ChainResidueDetails
ACYS462
BCYS462

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU329
ATHR330

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU329
BTHR330

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PDB entries from 2024-07-10

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