Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3A4Z

Structure of cytochrome P450 Vdh mutant (Vdh-K1) obtained by directed evolution

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	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	0046872	molecular_function	metal ion binding
A	0047748	molecular_function	cholestanetetraol 26-dehydrogenase activity
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
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	0046872	molecular_function	metal ion binding
B	0047748	molecular_function	cholestanetetraol 26-dehydrogenase activity
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
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	0046872	molecular_function	metal ion binding
C	0047748	molecular_function	cholestanetetraol 26-dehydrogenase activity
D	0004497	molecular_function	monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
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	0046872	molecular_function	metal ion binding
D	0047748	molecular_function	cholestanetetraol 26-dehydrogenase activity
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0005737	cellular_component	cytoplasm
E	0016491	molecular_function	oxidoreductase activity
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
E	0047748	molecular_function	cholestanetetraol 26-dehydrogenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM A 412

Chain	Residue
A	PHE58
A	VAL283
A	PRO287
A	ARG289
A	LEU312
A	PHE339
A	PHE340
A	GLY341
A	ILE344
A	HIS345
A	CYS347
A	LYS65
A	GLY349
A	ALA353
A	HOH425
A	ILE88
A	HIS95
A	ARG99
A	PHE106
A	ALA236
A	THR240
A	THR241

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 2501

Chain	Residue
A	ASP204
A	HOH580
A	HOH582
A	HOH601
A	HOH768
A	GOL3002

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 2505

Chain	Residue
A	GLY128
A	HOH610
A	HOH690
A	HOH795
A	HOH796

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 2506

Chain	Residue
A	ASP320
D	ASP320

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 4006

Chain	Residue
A	HIS342
A	GLY343
A	PHE346
A	HOH573
A	HOH594
A	HOH613

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 3001

Chain	Residue
A	ASP53
A	GLU56
A	HOH427
A	HOH558
D	ARG55
D	HOH462

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 3002

Chain	Residue
A	ASP204
A	HOH552
A	HOH768
A	CA2501
E	ARG70
E	PRO72
E	ALA304

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM B 412

Chain	Residue
B	PHE58
B	LYS65
B	ILE88
B	HIS95
B	ARG99
B	PHE106
B	ALA236
B	THR240
B	THR241
B	VAL283
B	PRO287
B	ARG289
B	LEU312
B	PHE339
B	PHE340
B	GLY341
B	ILE344
B	HIS345
B	CYS347
B	ALA353
B	HOH419

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM C 412

Chain	Residue
C	PHE58
C	LYS65
C	MET87
C	ILE88
C	HIS95
C	ARG99
C	PHE106
C	LEU233
C	ALA236
C	THR240
C	THR241
C	ARG289
C	LEU312
C	PHE339
C	PHE340
C	GLY341
C	ILE344
C	HIS345
C	CYS347
C	GLY349
C	ALA353
C	HOH433

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 2503

Chain	Residue
C	HOH429
C	HOH436
C	HOH466
C	ACT4004
C	ASP204
C	HOH428

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 4004

Chain	Residue
A	ARG70
A	PRO72
C	ASP204
C	HOH428
C	HOH477
C	CA2503

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT C 4007

Chain	Residue
C	HIS342
C	GLY343
C	PHE346
C	HOH489

site_id	BC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM D 412

Chain	Residue
D	PHE58
D	LYS65
D	ILE88
D	HIS95
D	ARG99
D	PHE106
D	LEU232
D	ALA236
D	THR240
D	THR241
D	VAL283
D	PRO287
D	ARG289
D	LEU312
D	PHE339
D	PHE340
D	GLY341
D	HIS345
D	CYS347
D	ALA353
D	HOH446

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA D 2502

Chain	Residue
B	HOH649
D	ASP204

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT D 4001

Chain	Residue
D	HIS342
D	GLY343
D	PHE346
D	HOH454
D	HOH485

site_id	BC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM E 412

Chain	Residue
E	PHE58
E	LYS65
E	MET87
E	ILE88
E	HIS95
E	ARG99
E	PHE106
E	ALA236
E	THR240
E	THR241
E	VAL283
E	PRO287
E	ARG289
E	LEU312
E	PHE339
E	PHE340
E	GLY341
E	HIS345
E	CYS347
E	LEU348
E	ALA353
E	HOH438

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 2504

Chain	Residue
C	HOH423
E	ASP204
E	HOH458
E	HOH792
E	ACT4005

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT E 4005

Chain	Residue
C	ARG70
E	ASP204
E	HOH747
E	CA2504

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT E 4008

Chain	Residue
E	HIS342
E	GLY343
E	PHE346

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE340-GLY349

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P0A512","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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