Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6T0F

Crystal structure of CYP124 in complex with cholest-4-en-3-one

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006707	biological_process	cholesterol catabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0010430	biological_process	fatty acid omega-oxidation
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	0031073	molecular_function	cholesterol 26-hydroxylase activity
A	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
A	0046872	molecular_function	metal ion binding
A	0070402	molecular_function	NADPH binding
A	0097089	biological_process	methyl-branched fatty acid metabolic process
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006707	biological_process	cholesterol catabolic process
B	0008395	molecular_function	steroid hydroxylase activity
B	0010430	biological_process	fatty acid omega-oxidation
B	0016491	molecular_function	oxidoreductase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0020037	molecular_function	heme binding
B	0031073	molecular_function	cholesterol 26-hydroxylase activity
B	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
B	0046872	molecular_function	metal ion binding
B	0070402	molecular_function	NADPH binding
B	0097089	biological_process	methyl-branched fatty acid metabolic process
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006707	biological_process	cholesterol catabolic process
C	0008395	molecular_function	steroid hydroxylase activity
C	0010430	biological_process	fatty acid omega-oxidation
C	0016491	molecular_function	oxidoreductase activity
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0020037	molecular_function	heme binding
C	0031073	molecular_function	cholesterol 26-hydroxylase activity
C	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
C	0046872	molecular_function	metal ion binding
C	0070402	molecular_function	NADPH binding
C	0097089	biological_process	methyl-branched fatty acid metabolic process
D	0004497	molecular_function	monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006707	biological_process	cholesterol catabolic process
D	0008395	molecular_function	steroid hydroxylase activity
D	0010430	biological_process	fatty acid omega-oxidation
D	0016491	molecular_function	oxidoreductase activity
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	0020037	molecular_function	heme binding
D	0031073	molecular_function	cholesterol 26-hydroxylase activity
D	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
D	0046872	molecular_function	metal ion binding
D	0070402	molecular_function	NADPH binding
D	0097089	biological_process	methyl-branched fatty acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	binding site for residue HEM A 501

Chain	Residue
A	ILE111
A	THR272
A	PRO314
A	VAL315
A	ARG320
A	TYR343
A	GLY370
A	PHE371
A	GLY372
A	HIS377
A	CYS379
A	HIS118
A	LEU380
A	GLY381
A	ALA385
A	K2B502
A	HOH660
A	HOH664
A	HOH695
A	HOH712
A	ARG122
A	PHE129
A	ILE176
A	LEU264
A	ALA267
A	GLY268
A	THR271

site_id	AC2
Number of Residues	11
Details	binding site for residue K2B A 502

Chain	Residue
A	PHE63
A	ASN93
A	THR95
A	ASN97
A	GLN99
A	LEU103
A	ILE197
A	PHE209
A	PHE212
A	HEM501
A	HOH547

site_id	AC3
Number of Residues	11
Details	binding site for residue MPO A 503

Chain	Residue
A	GLY181
A	PRO183
A	TYR222
A	ALA225
A	LEU226
A	ASP229
A	ARG230
A	HOH653
A	HOH832
A	HOH878
A	HOH908

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	GLU25
A	LEU26
A	GLY27
A	TRP55
A	PRO56

site_id	AC5
Number of Residues	3
Details	binding site for residue GOL A 505

Chain	Residue
A	HIS-1
A	HIS0
A	HOH868

site_id	AC6
Number of Residues	2
Details	binding site for residue GOL A 506

Chain	Residue
A	GOL507
A	HOH850

site_id	AC7
Number of Residues	2
Details	binding site for residue GOL A 507

Chain	Residue
A	GOL506
A	HOH1031

site_id	AC8
Number of Residues	15
Details	binding site for residue PGE A 508

Chain	Residue
A	ASP36
A	HIS278
A	LEU281
A	ARG285
A	PRO409
A	ARG411
A	HIS418
A	GLY419
A	HOH621
A	HOH633
A	HOH675
A	HOH704
A	HOH816
A	HOH894
A	HOH968

site_id	AC9
Number of Residues	4
Details	binding site for residue GOL A 509

Chain	Residue
A	SER165
A	GLU166
D	ASN233
D	HOH975

site_id	AD1
Number of Residues	23
Details	binding site for residue HEM B 501

Chain	Residue
B	HOH678
B	HOH714
B	HOH765
B	HOH850
B	ILE111
B	HIS118
B	ARG122
B	LEU264
B	ALA267
B	THR271
B	THR272
B	VAL315
B	ARG320
B	TYR343
B	GLY370
B	PHE371
B	GLY372
B	HIS377
B	CYS379
B	LEU380
B	GLY381
B	ALA385
B	K2B502

site_id	AD2
Number of Residues	12
Details	binding site for residue K2B B 502

Chain	Residue
B	PHE63
B	ASN93
B	THR95
B	ASN97
B	GLN99
B	LEU103
B	ILE197
B	PHE209
B	PHE212
B	PHE416
B	HEM501
B	HOH547

site_id	AD3
Number of Residues	13
Details	binding site for residue MPO B 503

Chain	Residue
B	GLY181
B	PRO183
B	TYR222
B	ALA225
B	LEU226
B	ASP229
B	ARG230
B	HIS235
B	HOH639
B	HOH700
B	HOH883
B	HOH929
B	HOH1019

site_id	AD4
Number of Residues	6
Details	binding site for residue GOL B 504

Chain	Residue
B	GLU25
B	LEU26
B	GLY27
B	SER28
B	TRP55
B	PRO56

site_id	AD5
Number of Residues	3
Details	binding site for residue GOL B 505

Chain	Residue
B	HOH627
B	HOH648
B	HOH979

site_id	AD6
Number of Residues	3
Details	binding site for residue GOL B 506

Chain	Residue
B	HIS0
B	HOH615
B	HOH1070

site_id	AD7
Number of Residues	12
Details	binding site for residue PGE B 507

Chain	Residue
B	ASP35
B	ASP36
B	HIS278
B	PRO409
B	ARG411
B	HIS418
B	GLY419
B	ILE420
B	PGE508
B	HOH605
B	HOH823
B	HOH975

site_id	AD8
Number of Residues	12
Details	binding site for residue PGE B 508

Chain	Residue
B	ARG10
B	PRO16
B	ASP36
B	ASP37
B	ASP40
B	ARG285
B	PGE507
B	HOH605
B	HOH655
B	HOH668
B	HOH970
B	HOH1046

site_id	AD9
Number of Residues	24
Details	binding site for residue HEM C 501

Chain	Residue
C	ILE111
C	HIS118
C	ARG122
C	LEU264
C	ALA267
C	THR271
C	THR272
C	PRO314
C	VAL315
C	ARG320
C	TYR343
C	GLY370
C	PHE371
C	GLY372
C	HIS377
C	CYS379
C	LEU380
C	GLY381
C	ALA385
C	K2B502
C	HOH687
C	HOH725
C	HOH727
C	HOH808

site_id	AE1
Number of Residues	11
Details	binding site for residue K2B C 502

Chain	Residue
C	PHE63
C	ASN93
C	THR95
C	ASN97
C	GLN99
C	LEU103
C	ILE197
C	PHE209
C	PHE212
C	HEM501
C	HOH547

site_id	AE2
Number of Residues	11
Details	binding site for residue MPO C 503

Chain	Residue
C	GLY181
C	PRO183
C	TYR222
C	ALA225
C	ASP229
C	ARG230
C	HOH697
C	HOH746
C	HOH923
C	HOH958
C	HOH1003

site_id	AE3
Number of Residues	3
Details	binding site for residue GOL C 504

Chain	Residue
C	GOL505
C	HOH692
C	HOH1155

site_id	AE4
Number of Residues	5
Details	binding site for residue GOL C 505

Chain	Residue
C	ASP291
C	SER295
C	GOL504
C	HOH924
C	HOH1046

site_id	AE5
Number of Residues	17
Details	binding site for residue PGE C 506

Chain	Residue
C	ARG10
C	THR14
C	PRO16
C	ASP36
C	ASP37
C	ASP40
C	ARG285
C	HOH617
C	HOH677
C	HOH709
C	HOH710
C	HOH821
C	HOH936
C	HOH960
C	HOH1005
C	HOH1033
C	HOH1037

site_id	AE6
Number of Residues	5
Details	binding site for residue PGE C 507

Chain	Residue
C	GLY108
C	LEU113
C	ARG117
C	HOH726
C	HOH815

site_id	AE7
Number of Residues	24
Details	binding site for residue HEM D 501

Chain	Residue
D	ILE111
D	HIS118
D	ARG122
D	LEU264
D	ALA267
D	GLY268
D	THR271
D	THR272
D	PRO314
D	VAL315
D	ARG320
D	TYR343
D	GLY370
D	PHE371
D	GLY372
D	HIS377
D	CYS379
D	GLY381
D	ALA385
D	K2B502
D	HOH680
D	HOH682
D	HOH685
D	HOH703

site_id	AE8
Number of Residues	11
Details	binding site for residue K2B D 502

Chain	Residue
D	PHE63
D	ASN93
D	THR95
D	ASN97
D	GLN99
D	LEU103
D	ILE197
D	PHE209
D	PHE212
D	HEM501
D	HOH547

site_id	AE9
Number of Residues	14
Details	binding site for residue MPO D 503

Chain	Residue
D	GLY181
D	PRO183
D	TYR222
D	ALA225
D	LEU226
D	ASP229
D	ARG230
D	HIS235
D	HOH617
D	HOH750
D	HOH949
D	HOH958
D	HOH984
D	HOH1105

site_id	AF1
Number of Residues	11
Details	binding site for residue PGE D 504

Chain	Residue
D	GLY108
D	SER109
D	VAL112
D	LEU113
D	ARG117
D	GOL506
D	HOH667
D	HOH818
D	HOH834
D	HOH951
D	HOH1170

site_id	AF2
Number of Residues	5
Details	binding site for residue GOL D 505

Chain	Residue
D	GLU25
D	LEU26
D	GLY27
D	TRP55
D	PRO56

site_id	AF3
Number of Residues	6
Details	binding site for residue GOL D 506

Chain	Residue
D	SER253
D	ARG255
D	GLU256
D	PGE504
D	HOH624
D	HOH647

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"19933331","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WM4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WM5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)