5VBU

Crystal Structure of Human Cytochrome P450 21A2 Hydroxyprogesterone Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0004509	molecular_function	steroid 21-monooxygenase activity
A	0005496	molecular_function	steroid binding
A	0005506	molecular_function	iron ion binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006694	biological_process	steroid biosynthetic process
A	0006704	biological_process	glucocorticoid biosynthetic process
A	0006705	biological_process	mineralocorticoid biosynthetic process
A	0008202	biological_process	steroid metabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0016020	cellular_component	membrane
A	0016125	biological_process	sterol metabolic process
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0020037	molecular_function	heme binding
A	0042445	biological_process	hormone metabolic process
A	0046872	molecular_function	metal ion 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	0005496	molecular_function	steroid binding
B	0005506	molecular_function	iron ion binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006694	biological_process	steroid biosynthetic process
B	0006704	biological_process	glucocorticoid biosynthetic process
B	0006705	biological_process	mineralocorticoid biosynthetic process
B	0008202	biological_process	steroid metabolic process
B	0008395	molecular_function	steroid hydroxylase activity
B	0016020	cellular_component	membrane
B	0016125	biological_process	sterol metabolic process
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0020037	molecular_function	heme binding
B	0042445	biological_process	hormone metabolic process
B	0046872	molecular_function	metal ion 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	0005496	molecular_function	steroid binding
C	0005506	molecular_function	iron ion binding
C	0005783	cellular_component	endoplasmic reticulum
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006694	biological_process	steroid biosynthetic process
C	0006704	biological_process	glucocorticoid biosynthetic process
C	0006705	biological_process	mineralocorticoid biosynthetic process
C	0008202	biological_process	steroid metabolic process
C	0008395	molecular_function	steroid hydroxylase activity
C	0016020	cellular_component	membrane
C	0016125	biological_process	sterol metabolic process
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0020037	molecular_function	heme binding
C	0042445	biological_process	hormone metabolic process
C	0046872	molecular_function	metal ion binding
C	0103069	molecular_function	17-hydroxyprogesterone 21-hydroxylase activity
C	0106309	molecular_function	progesterone 21-hydroxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue HEM A 501

Chain	Residue
A	ARG92
A	VAL359
A	VAL360
A	HIS366
A	ALA421
A	PHE422
A	ARG427
A	CYS429
A	LEU430
A	GLY431
A	SER109
A	TRP117
A	ILE173
A	LEU289
A	GLY292
A	GLY293
A	THR296
A	THR300

---

site_id	AC2
Number of Residues	10
Details	binding site for residue 3QZ A 502

Chain	Residue
A	VAL101
A	SER109
A	VAL198
A	ILE231
A	ARG234
A	ASP288
A	ILE291
A	GLY292
A	VAL360
A	LEU364

---

site_id	AC3
Number of Residues	21
Details	binding site for residue HEM B 501

Chain	Residue
B	ARG92
B	SER109
B	TRP117
B	LYS121
B	ILE173
B	LEU289
B	GLY292
B	GLY293
B	THR296
B	THR300
B	VAL359
B	VAL360
B	HIS366
B	LEU389
B	ALA421
B	PHE422
B	ARG427
B	CYS429
B	LEU430
B	GLY431
B	3QZ502

---

site_id	AC4
Number of Residues	10
Details	binding site for residue 3QZ B 502

Chain	Residue
B	VAL101
B	SER109
B	VAL198
B	ILE231
B	ARG234
B	ASP288
B	ILE291
B	GLY292
B	LEU364
B	HEM501

---

site_id	AC5
Number of Residues	22
Details	binding site for residue HEM C 501

Chain	Residue
C	ARG92
C	SER109
C	TRP117
C	LYS121
C	ILE173
C	LEU289
C	GLY292
C	GLY293
C	THR296
C	THR300
C	VAL359
C	VAL360
C	LEU364
C	HIS366
C	LEU389
C	ALA421
C	PHE422
C	ARG427
C	CYS429
C	LEU430
C	GLY431
C	3QZ502

---

site_id	AC6
Number of Residues	11
Details	binding site for residue 3QZ C 502

Chain	Residue
C	VAL101
C	SER109
C	VAL198
C	TRP202
C	ILE231
C	ARG234
C	ASP288
C	GLY292
C	VAL360
C	LEU364
C	HEM501

---

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	PHE422-GLY431

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	15
Details	BINDING: BINDING => ECO:0000269|PubMed:25855791, ECO:0007744|PDB:4Y8W

Chain	Residue	Details
A	ARG92
B	ARG427
C	ARG92
C	LYS121
C	ARG234
C	HIS366
C	ARG427
A	LYS121
A	ARG234
A	HIS366
A	ARG427
B	ARG92
B	LYS121
B	ARG234
B	HIS366

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: axial binding residue => ECO:0000269|PubMed:25855791, ECO:0007744|PDB:4Y8W

Chain	Residue	Details
A	CYS429
B	CYS429
C	CYS429

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