Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QZ1

Crystal Structure of Bovine Steroid of 21-hydroxylase (P450c21)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0004509	molecular_function	steroid 21-monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006694	biological_process	steroid biosynthetic process
A	0006704	biological_process	glucocorticoid biosynthetic process
A	0008202	biological_process	steroid metabolic process
A	0008395	molecular_function	steroid hydroxylase 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	0103069	molecular_function	17-hydroxyprogesterone 21-hydroxylase activity
A	0106309	molecular_function	progesterone 21-hydroxylase activity
B	0004497	molecular_function	monooxygenase activity
B	0004509	molecular_function	steroid 21-monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006694	biological_process	steroid biosynthetic process
B	0006704	biological_process	glucocorticoid biosynthetic process
B	0008202	biological_process	steroid metabolic process
B	0008395	molecular_function	steroid hydroxylase 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	0103069	molecular_function	17-hydroxyprogesterone 21-hydroxylase activity
B	0106309	molecular_function	progesterone 21-hydroxylase activity
C	0004497	molecular_function	monooxygenase activity
C	0004509	molecular_function	steroid 21-monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006694	biological_process	steroid biosynthetic process
C	0006704	biological_process	glucocorticoid biosynthetic process
C	0008202	biological_process	steroid metabolic process
C	0008395	molecular_function	steroid hydroxylase 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	0103069	molecular_function	17-hydroxyprogesterone 21-hydroxylase activity
C	0106309	molecular_function	progesterone 21-hydroxylase activity
D	0004497	molecular_function	monooxygenase activity
D	0004509	molecular_function	steroid 21-monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006694	biological_process	steroid biosynthetic process
D	0006704	biological_process	glucocorticoid biosynthetic process
D	0008202	biological_process	steroid metabolic process
D	0008395	molecular_function	steroid hydroxylase 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	0103069	molecular_function	17-hydroxyprogesterone 21-hydroxylase activity
D	0106309	molecular_function	progesterone 21-hydroxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM A 500

Chain	Residue
A	ARG92
A	LEU352
A	ALA361
A	LEU362
A	HIS364
A	LEU387
A	ALA419
A	PHE420
A	ARG425
A	VAL426
A	CYS427
A	ILE108
A	LEU428
A	GLY429
A	ALA433
A	3QZ501
A	SER109
A	TRP117
A	LEU128
A	GLY291
A	THR294
A	THR295
A	THR298

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3QZ A 501

Chain	Residue
A	LEU110
A	LEU196
A	TRP200
A	ARG232
A	GLY290
A	THR294
A	VAL358
A	HEM500

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 3QZ A 502

Chain	Residue
A	LEU64
A	GLN67
A	ILE95
A	GLN206
A	VAL382

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM B 500

Chain	Residue
B	ARG92
B	ILE108
B	SER109
B	TRP117
B	LYS121
B	LEU128
B	GLY291
B	THR294
B	THR295
B	THR298
B	VAL358
B	LEU362
B	HIS364
B	LEU387
B	ALA419
B	PHE420
B	ARG425
B	CYS427
B	LEU428
B	GLY429
B	ALA433
B	3QZ501

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3QZ B 501

Chain	Residue
B	SER109
B	LEU110
B	LEU196
B	TRP200
B	ILE229
B	ARG232
B	GLY290
B	THR294
B	VAL358
B	VAL469
B	HEM500

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 3QZ B 502

Chain	Residue
B	LEU40
B	LEU64
B	GLN206
B	MET210
B	LEU360

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM C 500

Chain	Residue
C	ARG92
C	ILE108
C	SER109
C	GLY291
C	THR294
C	THR295
C	THR298
C	LEU352
C	VAL358
C	HIS364
C	LEU387
C	ALA419
C	PHE420
C	ARG425
C	CYS427
C	LEU428
C	GLY429
C	ALA433
C	3QZ501
C	HOH606

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3QZ C 501

Chain	Residue
C	ARG232
C	ASP286
C	THR294
C	HEM500
C	VAL101
C	SER109
C	LEU196
C	TRP200
C	ILE229

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 3QZ C 502

Chain	Residue
C	GLN206
C	LEU360
C	ALA361
C	CYS467
C	GLY468

site_id	BC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM D 500

Chain	Residue
D	ARG92
D	SER109
D	TRP117
D	LYS121
D	GLY291
D	THR294
D	THR295
D	THR298
D	VAL358
D	ALA361
D	HIS364
D	LEU387
D	ALA419
D	PHE420
D	ARG425
D	VAL426
D	CYS427
D	LEU428
D	GLY429
D	3QZ501

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 3QZ D 501

Chain	Residue
D	SER109
D	LEU196
D	TRP200
D	ARG232
D	ASP286
D	THR294
D	HEM500

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 3QZ D 502

Chain	Residue
D	LEU64
D	GLY65
D	GLN206
D	LEU360
D	ALA361
D	CYS467

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE420-GLY429

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22262854","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QZ1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P08686","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22262854","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QZ1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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