2VKU

4,4'-Dihydroxybenzophenone Mimics Sterol Substrate in the Binding Site of Sterol 14alpha-Demethylase (CYP51) in the X-ray Structure of the Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006694	biological_process	steroid biosynthetic process
A	0008202	biological_process	steroid metabolic process
A	0008398	molecular_function	sterol 14-demethylase activity
A	0016125	biological_process	sterol metabolic process
A	0016126	biological_process	sterol biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DBE A1446

Chain	Residue
A	HIS16
A	GLY107
A	MET110
A	LEU179
A	PRO187
A	ALA398
A	HOH2514
A	HOH2515

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DBE A1447

Chain	Residue
A	MET99
A	MET225
A	PHE241
A	MET249
A	SER252
A	MET253
A	HEM1450
A	ARG96

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DBE A1448

Chain	Residue
A	ARG192
A	GLU308
A	LYS312
A	PHE387
A	GLY388
A	ARG393
A	ILE401
A	SO41452
A	HOH2518

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DBE A1449

Chain	Residue
A	TYR76
A	MET79
A	PHE83
A	ARG96
A	PHE255
A	HIS259
A	ILE323
A	MET433
A	HEM1450
A	HOH2367

---

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM A1450

Chain	Residue
A	TYR76
A	ARG96
A	ALA256
A	GLY257
A	THR260
A	SER261
A	THR264
A	PRO320
A	LEU321
A	LEU324
A	ARG326
A	PRO386
A	PHE387
A	GLY388
A	CYS394
A	PHE399
A	DBE1447
A	DBE1449
A	HOH2098
A	HOH2316
A	HOH2445

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A1452

Chain	Residue
A	ARG193
A	ARG381
A	ALA389
A	GLY390
A	ARG393
A	DBE1448
A	HOH2254
A	HOH2437
A	HOH2502

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A1453

Chain	Residue
A	ARG64
A	ARG193
A	ARG381
A	HOH2503

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A1454

Chain	Residue
A	THR236
A	GLY237
A	ARG294
A	HOH2505
A	HOH2506
A	HOH2507
A	HOH2508
A	HOH2509

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A1455

Chain	Residue
A	ARG23
A	HIS101
A	ARG106
A	GLY107
A	HOH2146
A	HOH2511

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A1456

Chain	Residue
A	HIS275
A	ARG276
A	ASP277
A	ALA278

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A1457

Chain	Residue
A	ARG174
A	LYS432
A	HOH2513

---

Functional Information from PROSITE/UniProt

site_id	PS00086
Number of Residues	10
Details	CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGRHRCVG

Chain	Residue	Details
A	PHE387-GLY396

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11248033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15530358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17846131","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19190730","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"PDB data bank","title":"Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from Mycobacterium tuberculosis.","authors":["Podust L.M.","Yermalitskaya L.V.","Kim Y.","Waterman M.R."]}},{"source":"PDB","id":"1E9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X8V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11248033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15530358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17846131","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19190730","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"PDB data bank","title":"Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from Mycobacterium tuberculosis.","authors":["Podust L.M.","Yermalitskaya L.V.","Kim Y.","Waterman M.R."]}},{"source":"PDB","id":"1E9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X8V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
A	HIS259
A	THR260

---