6Y1T

The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with a Trp51 to S-Trp51 modification

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0006979	biological_process	response to oxidative stress
A	0020037	molecular_function	heme binding
A	0034599	biological_process	cellular response to oxidative stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue HEM A 301

Chain	Residue
A	PRO44
A	LEU177
A	GLY178
A	LYS179
A	THR180
A	HIS181
A	ASN184
A	SER185
A	TRP191
A	THR234
A	HOH448
A	4OG51
A	HOH467
A	HOH519
A	HOH570
A	PRO145
A	ASP146
A	ALA147
A	LEU171
A	MET172
A	ALA174
A	HIS175

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site_id	AC2
Number of Residues	2
Details	binding site for residue EDO A 302

Chain	Residue
A	LYS123
A	HOH483

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site_id	AC3
Number of Residues	9
Details	binding site for residue 1PE A 303

Chain	Residue
A	PHE89
A	GLU93
A	HIS96
A	PRO100
A	SER104
A	ASP132
A	HOH520
A	HOH539
A	HOH729

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Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL

Chain	Residue	Details
A	GLU167-LEU177

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site_id	PS00436
Number of Residues	12
Details	PEROXIDASE_2 Peroxidases active site signature. GPvlVRLaWHTS

Chain	Residue	Details
A	GLY43-SER54

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10722697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11170452","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2169873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6092361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8384877","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8673607","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 709

Chain	Residue	Details
A	ARG48	electrostatic stabiliser
A	THR56	electrostatic stabiliser, proton acceptor, proton donor
A	ASN195	single electron acceptor, single electron donor

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