8PVD

Structure of catalase determined by cryoEM at 100 keV

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000302	biological_process	response to reactive oxygen species
A	0001649	biological_process	osteoblast differentiation
A	0001657	biological_process	ureteric bud development
A	0001666	biological_process	response to hypoxia
A	0001822	biological_process	kidney development
A	0004046	molecular_function	aminoacylase activity
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0005778	cellular_component	peroxisomal membrane
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0005925	cellular_component	focal adhesion
A	0006979	biological_process	response to oxidative stress
A	0009410	biological_process	response to xenobiotic stimulus
A	0009411	biological_process	response to UV
A	0009636	biological_process	response to toxic substance
A	0009642	biological_process	response to light intensity
A	0009650	biological_process	UV protection
A	0010193	biological_process	response to ozone
A	0010288	biological_process	response to lead ion
A	0014823	biological_process	response to activity
A	0014854	biological_process	response to inactivity
A	0016020	cellular_component	membrane
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0016684	molecular_function	oxidoreductase activity, acting on peroxide as acceptor
A	0019899	molecular_function	enzyme binding
A	0020037	molecular_function	heme binding
A	0032355	biological_process	response to estradiol
A	0032868	biological_process	response to insulin
A	0032991	cellular_component	protein-containing complex
A	0033189	biological_process	response to vitamin A
A	0033197	biological_process	response to vitamin E
A	0033591	biological_process	response to L-ascorbic acid
A	0034774	cellular_component	secretory granule lumen
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043066	biological_process	negative regulation of apoptotic process
A	0045471	biological_process	response to ethanol
A	0046686	biological_process	response to cadmium ion
A	0046872	molecular_function	metal ion binding
A	0050661	molecular_function	NADP binding
A	0051781	biological_process	positive regulation of cell division
A	0055093	biological_process	response to hyperoxia
A	0061692	biological_process	cellular detoxification of hydrogen peroxide
A	0070062	cellular_component	extracellular exosome
A	0070542	biological_process	response to fatty acid
A	0071363	biological_process	cellular response to growth factor stimulus
A	0072722	biological_process	response to amitrole
A	0080184	biological_process	response to phenylpropanoid
A	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PROSITE/UniProt

site_id	PS00437
Number of Residues	9
Details	CATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDTH

Chain	Residue	Details
A	ARG354-HIS362

---

site_id	PS00438
Number of Residues	17
Details	CATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG

Chain	Residue	Details
A	PHE64-GLY80

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"10656833","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10656833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10656833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10656833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10656833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10666617","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DGB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DGH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F4J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QQW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24270","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---