Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1B4L

15 ATMOSPHERE OXYGEN YEAST CU/ZN SUPEROXIDE DISMUTASE ROOM TEMPERATURE (298K) STRUCTURE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004784	molecular_function	superoxide dismutase activity
A	0005507	molecular_function	copper ion binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005758	cellular_component	mitochondrial intermembrane space
A	0005829	cellular_component	cytosol
A	0006801	biological_process	superoxide metabolic process
A	0006825	biological_process	copper ion transport
A	0006878	biological_process	intracellular copper ion homeostasis
A	0006882	biological_process	intracellular zinc ion homeostasis
A	0008270	molecular_function	zinc ion binding
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0016670	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor
A	0019430	biological_process	removal of superoxide radicals
A	0031505	biological_process	fungal-type cell wall organization
A	0034599	biological_process	cellular response to oxidative stress
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0050821	biological_process	protein stabilization
A	1901856	biological_process	negative regulation of cellular respiration
A	1902693	cellular_component	superoxide dismutase complex
A	1990748	biological_process	cellular detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 154

Chain	Residue
A	HIS46
A	HIS48
A	HIS63
A	HIS120

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 155

Chain	Residue
A	HIS63
A	HIS71
A	HIS80
A	ASP83

site_id	CU
Number of Residues	4
Details	COPPER BINDING SITE

Chain	Residue
A	CU154
A	HIS46
A	HIS48
A	HIS120

site_id	ZN
Number of Residues	5
Details	ZINC BINDING SITE

Chain	Residue
A	ZN155
A	HIS63
A	HIS71
A	HIS80
A	ASP83

Functional Information from PROSITE/UniProt

site_id	PS00087
Number of Residues	11
Details	SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHIHEfGDaT

Chain	Residue	Details
A	GLY44-THR54

site_id	PS00332
Number of Residues	12
Details	SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGpRpACgvI

Chain	Residue	Details
A	GLY138-ILE149

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"description":"in apo form","evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11524675","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8652572","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11524675","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15665377","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"15166219","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
A	ARG143
A	HIS63

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 2jcw

Chain	Residue	Details
A	HIS63

site_id	MCSA1
Number of Residues	8
Details	M-CSA 138

Chain	Residue	Details
A	HIS46	metal ligand
A	HIS48	metal ligand
A	HIS63	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
A	HIS71	metal ligand
A	HIS80	metal ligand
A	ASP83	metal ligand
A	HIS120	metal ligand
A	ARG143	electrostatic stabiliser, hydrogen bond donor

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