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2ZBY

Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (R84A mutant)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0070640biological_processvitamin D3 metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 413
ChainResidue
APHE95
AALA294
AARG297
AALA347
APHE348
AGLY349
AHIS353
ACYS355
AGLY357
AALA361
AHOH417
AILE96
AHOH438
AHOH463
AHOH584
AHIS103
AARG107
ALEU241
AALA244
ATHR248
ATHR249
AILE290

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGVHQCLG
ChainResidueDetails
APHE348-GLY357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18937506
ChainResidueDetails
ATHR81

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18314962
ChainResidueDetails
AHIS103
AARG107
ASER236
AARG297
AHIS353

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18314962, ECO:0000269|PubMed:18937506
ChainResidueDetails
AARG193
AILE293

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:18314962
ChainResidueDetails
ACYS355

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
ATHR248
AGLU247

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PDB entries from 2024-07-24

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