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2ZBX

Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (wild type) with imidazole bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 413
ChainResidue
APHE95
AARG297
AALA347
APHE348
AGLY349
AHIS353
ACYS355
ALEU356
AGLY357
AHOH512
AHOH532
AILE96
AHOH557
AHOH741
AHIS103
AARG107
APHE114
AALA244
ATHR248
AMET252
AALA294

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IMD A 501
ChainResidue
AALA244
ATHR248

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 site: {"evidences":[{"source":"PubMed","id":"18937506","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18314962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18314962","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18937506","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"18314962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

246704

PDB entries from 2025-12-24

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