Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2IJ7

Structure of Mycobacterium tuberculosis CYP121 in complex with the antifungal drug fluconazole

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
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
B	0006707	biological_process	cholesterol catabolic process
B	0008395	molecular_function	steroid hydroxylase activity
B	0009975	molecular_function	cyclase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	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
B	0020037	molecular_function	heme binding
B	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
B	0046872	molecular_function	metal ion binding
B	0070025	molecular_function	carbon monoxide binding
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
C	0006707	biological_process	cholesterol catabolic process
C	0008395	molecular_function	steroid hydroxylase activity
C	0009975	molecular_function	cyclase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	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
C	0020037	molecular_function	heme binding
C	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
C	0046872	molecular_function	metal ion binding
C	0070025	molecular_function	carbon monoxide binding
D	0004497	molecular_function	monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
D	0006707	biological_process	cholesterol catabolic process
D	0008395	molecular_function	steroid hydroxylase activity
D	0009975	molecular_function	cyclase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	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
D	0020037	molecular_function	heme binding
D	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
D	0046872	molecular_function	metal ion binding
D	0070025	molecular_function	carbon monoxide binding
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0005737	cellular_component	cytoplasm
E	0006707	biological_process	cholesterol catabolic process
E	0008395	molecular_function	steroid hydroxylase activity
E	0009975	molecular_function	cyclase activity
E	0016491	molecular_function	oxidoreductase activity
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	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
E	0020037	molecular_function	heme binding
E	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
E	0046872	molecular_function	metal ion binding
E	0070025	molecular_function	carbon monoxide binding
F	0004497	molecular_function	monooxygenase activity
F	0005506	molecular_function	iron ion binding
F	0005737	cellular_component	cytoplasm
F	0006707	biological_process	cholesterol catabolic process
F	0008395	molecular_function	steroid hydroxylase activity
F	0009975	molecular_function	cyclase activity
F	0016491	molecular_function	oxidoreductase activity
F	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
F	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
F	0020037	molecular_function	heme binding
F	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
F	0046872	molecular_function	metal ion binding
F	0070025	molecular_function	carbon monoxide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM A 462

Chain	Residue
A	MET62
A	ARG286
A	ALA337
A	PHE338
A	GLY339
A	HIS343
A	CYS345
A	PRO346
A	TPF2472
A	HOH2527
A	HOH2583
A	MET86
A	HOH2661
A	HOH2792
A	HIS146
A	PHE230
A	GLY234
A	SER237
A	PHE241
A	PHE280
A	LEU284

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM B 462

Chain	Residue
B	MET62
B	MET86
B	HIS146
B	PHE230
B	GLY234
B	SER237
B	PHE280
B	LEU284
B	ARG286
B	ALA337
B	PHE338
B	GLY339
B	HIS343
B	CYS345
B	PRO346
B	GLY347
B	TPF2470
B	HOH2517
B	HOH2531
B	HOH2547
B	HOH2581
B	HOH2631
B	HOH2834

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM C 462

Chain	Residue
C	MET62
C	MET86
C	HIS146
C	PHE230
C	GLY234
C	SER237
C	PHE241
C	PHE280
C	LEU284
C	ARG286
C	ALA337
C	PHE338
C	GLY339
C	HIS343
C	CYS345
C	PRO346
C	GLY347
C	TPF2471
C	HOH2477
C	HOH2494
C	HOH2516
C	HOH2522
C	HOH2598
C	HOH2701

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM D 462

Chain	Residue
D	MET62
D	MET86
D	HIS146
D	PHE230
D	GLY234
D	SER237
D	PHE241
D	PHE280
D	LEU284
D	ARG286
D	ALA337
D	PHE338
D	GLY339
D	GLN342
D	HIS343
D	CYS345
D	PRO346
D	TPF2473
D	HOH2601
D	HOH2623
D	HOH2658
D	HOH2748

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM E 462

Chain	Residue
E	ARG286
E	ALA337
E	PHE338
E	GLY339
E	HIS343
E	CYS345
E	PRO346
E	HOH481
E	HOH483
E	HOH615
E	HOH849
E	MET62
E	MET86
E	ARG95
E	HIS146
E	PHE230
E	GLY234
E	SER237
E	PHE280
E	LEU284

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM F 462

Chain	Residue
F	MET62
F	MET86
F	HIS146
F	PHE230
F	GLY234
F	SER237
F	THR238
F	PHE280
F	LEU284
F	ARG286
F	ALA337
F	PHE338
F	GLY339
F	HIS343
F	CYS345
F	PRO346
F	TPF2474
F	HOH2520
F	HOH2617
F	HOH2620
F	HOH2648
F	HOH2764

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TPF B 2470

Chain	Residue
B	THR77
B	VAL82
B	VAL83
B	ASN85
B	MET86
B	ALA167
B	PHE168
B	THR229
B	GLN385
B	HEM462
B	HOH2547
B	HOH2654
B	HOH2677
B	HOH2834

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TPF C 2471

Chain	Residue
C	THR77
C	VAL83
C	ASN85
C	MET86
C	ALA167
C	PHE168
C	GLN385
C	ARG386
C	HEM462
C	HOH2494
C	HOH2516
C	HOH2522
C	HOH2624
C	HOH2692

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE TPF A 2472

Chain	Residue
A	THR77
A	VAL83
A	ASN85
A	MET86
A	ALA167
A	PHE168
A	THR229
A	ALA233
A	SER237
A	PHE280
A	GLN385
A	ARG386
A	HEM462
A	HOH2509
A	HOH2519
A	HOH2553
A	HOH2583
A	HOH2661
A	HOH2761
A	HOH2762
A	HOH2792

site_id	BC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE TPF D 2473

Chain	Residue
D	THR77
D	VAL83
D	ASN85
D	MET86
D	ALA167
D	PHE168
D	THR229
D	ALA233
D	SER237
D	GLN385
D	ARG386
D	HEM462
D	HOH2516
D	HOH2601
D	HOH2652
D	HOH2658
D	HOH2667
D	HOH2748

site_id	BC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE TPF F 2474

Chain	Residue
F	THR77
F	VAL83
F	ASN85
F	MET86
F	ALA167
F	PHE168
F	THR229
F	ALA233
F	SER237
F	PHE280
F	GLN385
F	ARG386
F	HEM462
F	HOH2570
F	HOH2575
F	HOH2617
F	HOH2764

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	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:17028183, ECO:0000269\|PubMed:19416919

Chain	Residue	Details
B	LYS301
B	GLN385
C	THR77
C	SER237
C	LYS301
C	GLN385
D	THR77
D	SER237
D	LYS301
D	GLN385
E	THR77
E	SER237
E	LYS301
E	GLN385
F	THR77
F	SER237
F	LYS301
F	GLN385
A	THR77
A	SER237
A	LYS301
A	GLN385
B	THR77
B	SER237

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	ASN85
B	ASN85
C	ASN85
D	ASN85
E	ASN85
F	ASN85

site_id	SWS_FT_FI3
Number of Residues	12
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
B	ARG286
B	HIS343
C	ARG286
C	HIS343
D	ARG286
D	HIS343
E	ARG286
E	HIS343
F	ARG286
F	HIS343

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: axial binding residue

Chain	Residue	Details
A	CYS345
B	CYS345
C	CYS345
D	CYS345
E	CYS345
F	CYS345

site_id	SWS_FT_FI5
Number of Residues	12
Details	SITE: Participates in a stacking interactions with the tyrosyl of cYY

Chain	Residue	Details
D	PHE168
D	TRP182
E	PHE168
E	TRP182
F	PHE168
F	TRP182
A	PHE168
A	TRP182
B	PHE168
B	TRP182
C	PHE168
C	TRP182

site_id	SWS_FT_FI6
Number of Residues	6
Details	SITE: Important for the position of heme

Chain	Residue	Details
A	PRO346
B	PRO346
C	PRO346
D	PRO346
E	PRO346
F	PRO346

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