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3K9V

Crystal structure of rat mitochondrial P450 24A1 S57D in complex with CHAPS

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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 520
ChainResidue
AHOH4
ASER334
ATHR394
AARG396
APRO454
APHE455
AGLY456
AILE457
AARG460
AMET461
ACYS462
AARG128
AGLY464
ACPS600
ALEU147
ATRP155
AARG159
ALEU323
AALA326
AALA327
ATHR330

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CPS A 600
ChainResidue
ASER205
AASN208
ALYS243
AGLU329
ATHR394
AGLY499
AHEM520
AHOH584
AHOH597
AHOH618

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CPS A 601
ChainResidue
AGLN82
APHE104
ALEU129
ALYS132
AMET253
BLEU66

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CPS A 602
ChainResidue
BTRP64
BGLU72

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 520
ChainResidue
BARG128
BLEU147
BTRP155
BARG159
BLEU323
BALA326
BALA327
BTHR330
BSER334
BTHR394
BARG396
BPRO454
BPHE455
BGLY456
BILE457
BARG460
BMET461
BCYS462
BGLY464
BCPS700

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CPS B 700
ChainResidue
BTYR204
BMET246
BGLU329
BPHE393
BTHR394
BGLY499
BHEM520
BHOH599
BHOH619

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CPS B 701
ChainResidue
ALEU66
BPHE74
BLEU79
BPHE104
BMET253
BVAL254

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CPS B 702
ChainResidue
ATRP64
ATRP75
BARG262

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

219869

PDB entries from 2024-05-15

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