5OPA

The crystal structure of P450 CYP121 in complex with lead compound 7b

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0006707	biological_process	cholesterol catabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0009975	molecular_function	cyclase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0016717	molecular_function	oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
A	0020037	molecular_function	heme binding
A	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
A	0046872	molecular_function	metal ion binding
A	0070025	molecular_function	carbon monoxide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue SO4 A 401

Chain	Residue
A	LYS211
A	PRO330
A	ASN331
A	PRO332
A	THR333
A	SER334
A	HOH523
A	HOH704

---

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 402

Chain	Residue
A	ARG17
A	HOH505
A	HOH539
A	HOH608
A	SER12

---

site_id	AC3
Number of Residues	8
Details	binding site for residue SO4 A 403

Chain	Residue
A	ARG58
A	SER61
A	MET62
A	LYS63
A	HIS343
A	HOH556
A	HOH559
A	HOH703

---

site_id	AC4
Number of Residues	29
Details	binding site for residue HEM A 404

Chain	Residue
A	MET62
A	MET86
A	HIS146
A	PHE230
A	ALA233
A	GLY234
A	SER237
A	THR238
A	PHE241
A	PHE280
A	LEU284
A	ARG286
A	ALA337
A	PHE338
A	GLY339
A	HIS343
A	CYS345
A	PRO346
A	GLY347
A	GLY351
A	A2W405
A	SO4407
A	HOH521
A	HOH530
A	HOH534
A	HOH546
A	HOH593
A	HOH802
A	HOH866

---

site_id	AC5
Number of Residues	17
Details	binding site for residue A2W A 405

Chain	Residue
A	VAL78
A	VAL82
A	ASN85
A	ALA167
A	PHE168
A	TRP182
A	VAL228
A	THR229
A	GLY232
A	GLN385
A	HEM404
A	SO4407
A	HOH536
A	HOH545
A	HOH663
A	HOH768
A	HOH796

---

site_id	AC6
Number of Residues	8
Details	binding site for residue SO4 A 406

Chain	Residue
A	ARG134
A	ASN135
A	PHE161
A	ARG381
A	ARG391
A	HOH508
A	HOH528
A	HOH551

---

site_id	AC7
Number of Residues	6
Details	binding site for residue SO4 A 407

Chain	Residue
A	PHE168
A	ARG386
A	HEM404
A	A2W405
A	HOH541
A	HOH546

---

site_id	AC8
Number of Residues	11
Details	binding site for residue PEG A 408

Chain	Residue
A	SER165
A	ILE166
A	MET169
A	GLN377
A	LEU378
A	ARG391
A	PRO393
A	HOH527
A	HOH621
A	HOH854
A	HOH860

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE338-GLY347

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:19416919

Chain	Residue	Details
A	SER237
A	LYS301
A	GLN385
A	THR77

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	ASN85

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12435731, ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197, ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978, ECO:0000269|PubMed:23620594

Chain	Residue	Details
A	ARG286
A	HIS343

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: axial binding residue

Chain	Residue	Details
A	CYS345

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Participates in a stacking interactions with the tyrosyl of cYY

Chain	Residue	Details
A	PHE168
A	TRP182

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Important for the position of heme

Chain	Residue	Details
A	PRO346

---