6H08

The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with a His175Me-His proximal ligand substitution

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
B	0004601	molecular_function	peroxidase activity
B	0006979	biological_process	response to oxidative stress
B	0020037	molecular_function	heme binding
B	0034599	biological_process	cellular response to oxidative stress
C	0004601	molecular_function	peroxidase activity
C	0006979	biological_process	response to oxidative stress
C	0020037	molecular_function	heme binding
C	0034599	biological_process	cellular response to oxidative stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue HEM A 301

Chain	Residue
A	PRO44
A	GLY178
A	LYS179
A	THR180
A	HIS181
A	ASN184
A	SER185
A	TRP191
A	LEU232
A	HOH436
A	HOH439
A	VAL45
A	HOH459
A	HOH502
A	ARG48
A	TRP51
A	PRO145
A	ASP146
A	LEU171
A	ALA174
A	MHS175

---

site_id	AC2
Number of Residues	5
Details	binding site for residue CO A 302

Chain	Residue
A	HIS0
A	HIS2
A	HIS60
A	HOH524
A	HOH585

---

site_id	AC3
Number of Residues	6
Details	binding site for residue MN A 303

Chain	Residue
A	HIS1
A	HIS3
A	HOH441
A	HOH564
C	ASP34
C	HOH411

---

site_id	AC4
Number of Residues	7
Details	binding site for residue NA A 304

Chain	Residue
A	ASP34
A	HOH407
A	HOH533
B	HIS1
B	HIS3
B	NA301
B	HOH503

---

site_id	AC5
Number of Residues	7
Details	binding site for residue NA B 301

Chain	Residue
A	ASP34
A	NA304
A	HOH407
A	HOH533
B	HIS1
B	HIS3
B	HOH503

---

site_id	AC6
Number of Residues	21
Details	binding site for residue HEM B 302

Chain	Residue
B	PRO44
B	VAL45
B	ARG48
B	TRP51
B	PRO145
B	ASP146
B	LEU171
B	ALA174
B	MHS175
B	GLY178
B	LYS179
B	THR180
B	HIS181
B	ASN184
B	SER185
B	TRP191
B	LEU232
B	HOH415
B	HOH422
B	HOH461
B	HOH470

---

site_id	AC7
Number of Residues	4
Details	binding site for residue CO B 303

Chain	Residue
B	HIS-1
B	HIS-2
B	HOH588
B	HOH589

---

site_id	AC8
Number of Residues	6
Details	binding site for residue CO B 304

Chain	Residue
B	HIS0
B	HIS2
B	HIS60
B	HOH534
B	HOH550
B	HOH561

---

site_id	AC9
Number of Residues	22
Details	binding site for residue HEM C 301

Chain	Residue
C	PRO44
C	VAL45
C	ARG48
C	TRP51
C	PRO145
C	ASP146
C	LEU171
C	ALA174
C	MHS175
C	GLY178
C	LYS179
C	THR180
C	HIS181
C	ASN184
C	SER185
C	TRP191
C	LEU232
C	HOH402
C	HOH410
C	HOH412
C	HOH418
C	HOH449

---

site_id	AD1
Number of Residues	7
Details	binding site for residue CO C 302

Chain	Residue
B	ASP34
B	HOH407
B	HOH546
B	HOH547
C	HIS1
C	HIS3
C	HOH405

---

site_id	AD2
Number of Residues	6
Details	binding site for residue CO C 303

Chain	Residue
C	HIS0
C	HIS2
C	HIS60
C	HOH488
C	HOH568
C	HOH570

---

site_id	AD3
Number of Residues	3
Details	binding site for residue CO C 304

Chain	Residue
B	HOH624
C	HIS-1
C	HIS-2

---

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

---

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

Chain	Residue	Details
A	GLY43-SER54

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
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

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 709

Chain	Residue	Details
A	ARG48	electrostatic stabiliser
A	HIS52	electrostatic stabiliser, proton acceptor, proton donor
A	ASN195	single electron acceptor, single electron donor

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 709

Chain	Residue	Details
B	ARG48	electrostatic stabiliser
B	HIS52	electrostatic stabiliser, proton acceptor, proton donor
B	ASN195	single electron acceptor, single electron donor

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 709

Chain	Residue	Details
C	ARG48	electrostatic stabiliser
C	HIS52	electrostatic stabiliser, proton acceptor, proton donor
C	ASN195	single electron acceptor, single electron donor

---