Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4BCY

Monomeric Human Cu,Zn Superoxide dismutase, mutation H43F

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000303	biological_process	response to superoxide
A	0001541	biological_process	ovarian follicle development
A	0001819	biological_process	positive regulation of cytokine production
A	0001890	biological_process	placenta development
A	0001895	biological_process	retina homeostasis
A	0001975	biological_process	response to amphetamine
A	0002262	biological_process	myeloid cell homeostasis
A	0004784	molecular_function	superoxide dismutase activity
A	0005507	molecular_function	copper ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005758	cellular_component	mitochondrial intermembrane space
A	0005759	cellular_component	mitochondrial matrix
A	0005764	cellular_component	lysosome
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006749	biological_process	glutathione metabolic process
A	0006801	biological_process	superoxide metabolic process
A	0006879	biological_process	intracellular iron ion homeostasis
A	0006979	biological_process	response to oxidative stress
A	0007283	biological_process	spermatogenesis
A	0007566	biological_process	embryo implantation
A	0007605	biological_process	sensory perception of sound
A	0007626	biological_process	locomotory behavior
A	0008089	biological_process	anterograde axonal transport
A	0008090	biological_process	retrograde axonal transport
A	0008217	biological_process	regulation of blood pressure
A	0008270	molecular_function	zinc ion binding
A	0009408	biological_process	response to heat
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0019226	biological_process	transmission of nerve impulse
A	0019430	biological_process	removal of superoxide radicals
A	0019899	molecular_function	enzyme binding
A	0030141	cellular_component	secretory granule
A	0030346	molecular_function	protein phosphatase 2B binding
A	0031045	cellular_component	dense core granule
A	0031267	molecular_function	small GTPase binding
A	0031410	cellular_component	cytoplasmic vesicle
A	0031667	biological_process	response to nutrient levels
A	0032287	biological_process	peripheral nervous system myelin maintenance
A	0032839	cellular_component	dendrite cytoplasm
A	0032930	biological_process	positive regulation of superoxide anion generation
A	0032991	cellular_component	protein-containing complex
A	0033081	biological_process	regulation of T cell differentiation in thymus
A	0034465	biological_process	response to carbon monoxide
A	0034599	biological_process	cellular response to oxidative stress
A	0035865	biological_process	cellular response to potassium ion
A	0040014	biological_process	regulation of multicellular organism growth
A	0042542	biological_process	response to hydrogen peroxide
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043025	cellular_component	neuronal cell body
A	0043065	biological_process	positive regulation of apoptotic process
A	0043066	biological_process	negative regulation of apoptotic process
A	0043087	biological_process	regulation of GTPase activity
A	0043410	biological_process	positive regulation of MAPK cascade
A	0043524	biological_process	negative regulation of neuron apoptotic process
A	0045471	biological_process	response to ethanol
A	0046620	biological_process	regulation of organ growth
A	0046688	biological_process	response to copper ion
A	0046716	biological_process	muscle cell cellular homeostasis
A	0046872	molecular_function	metal ion binding
A	0048538	biological_process	thymus development
A	0048678	biological_process	response to axon injury
A	0050665	biological_process	hydrogen peroxide biosynthetic process
A	0050728	biological_process	negative regulation of inflammatory response
A	0050766	biological_process	positive regulation of phagocytosis
A	0051087	molecular_function	protein-folding chaperone binding
A	0051881	biological_process	regulation of mitochondrial membrane potential
A	0060047	biological_process	heart contraction
A	0060052	biological_process	neurofilament cytoskeleton organization
A	0060087	biological_process	relaxation of vascular associated smooth muscle
A	0060088	biological_process	auditory receptor cell stereocilium organization
A	0070062	cellular_component	extracellular exosome
A	0071276	biological_process	cellular response to cadmium ion
A	0071318	biological_process	cellular response to ATP
A	0072593	biological_process	reactive oxygen species metabolic process
A	0097332	biological_process	response to antipsychotic drug
A	1902177	biological_process	positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A	1904115	cellular_component	axon cytoplasm

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 1153

Chain	Residue
A	HIS46
A	HIS48
A	HIS63
A	HIS120
A	HOH2019

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 1154

Chain	Residue
A	HIS46
A	HIS48
A	HIS63
A	HIS120

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1155

Chain	Residue
A	HIS63
A	HIS71
A	HIS80
A	ASP83

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 1156

Chain	Residue
A	ALA1
A	GLU51
A	ASP96
A	HOH2069

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 1157

Chain	Residue
A	GLU78
A	GLU121

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD A 1158

Chain	Residue
A	GLU50
A	ASP52
A	ASP90
A	ASP92
A	CD1159

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 1159

Chain	Residue
A	ASP52
A	ASP90
A	CD1158
A	HOH2069

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 1160

Chain	Residue
A	HIS110
A	GLN153

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 1161

Chain	Residue
A	ASP109
A	HIS110
A	GLN153
A	HOH2070

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1162

Chain	Residue
A	LEU67
A	SER68
A	ARG69
A	LYS122

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 1163

Chain	Residue
A	HIS48
A	GLU50
A	GLY61

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY138-ILE149

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12963370","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17548825","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20727846","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"1463506","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7002610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
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":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07632","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"24140062","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"22496122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Cross-link: {"description":"1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)","evidences":[{"source":"PubMed","id":"20600836","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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