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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1BA9

THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0000303biological_processresponse to superoxide
A0001541biological_processovarian follicle development
A0001819biological_processpositive regulation of cytokine production
A0001890biological_processplacenta development
A0001895biological_processretina homeostasis
A0001975biological_processresponse to amphetamine
A0002262biological_processmyeloid cell homeostasis
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005759cellular_componentmitochondrial matrix
A0005764cellular_componentlysosome
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006749biological_processglutathione metabolic process
A0006801biological_processsuperoxide metabolic process
A0006879biological_processintracellular iron ion homeostasis
A0006979biological_processresponse to oxidative stress
A0007283biological_processspermatogenesis
A0007566biological_processembryo implantation
A0007605biological_processsensory perception of sound
A0007626biological_processlocomotory behavior
A0008089biological_processanterograde axonal transport
A0008090biological_processretrograde axonal transport
A0008217biological_processregulation of blood pressure
A0008270molecular_functionzinc ion binding
A0009408biological_processresponse to heat
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019226biological_processtransmission of nerve impulse
A0019430biological_processremoval of superoxide radicals
A0019899molecular_functionenzyme binding
A0030141cellular_componentsecretory granule
A0030346molecular_functionprotein phosphatase 2B binding
A0031045cellular_componentdense core granule
A0031267molecular_functionsmall GTPase binding
A0031410cellular_componentcytoplasmic vesicle
A0031667biological_processresponse to nutrient levels
A0032287biological_processperipheral nervous system myelin maintenance
A0032839cellular_componentdendrite cytoplasm
A0032930biological_processpositive regulation of superoxide anion generation
A0032991cellular_componentprotein-containing complex
A0033081biological_processregulation of T cell differentiation in thymus
A0034465biological_processresponse to carbon monoxide
A0034599biological_processcellular response to oxidative stress
A0035865biological_processcellular response to potassium ion
A0040014biological_processregulation of multicellular organism growth
A0042542biological_processresponse to hydrogen peroxide
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043025cellular_componentneuronal cell body
A0043065biological_processpositive regulation of apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0043087biological_processregulation of GTPase activity
A0043410biological_processpositive regulation of MAPK cascade
A0043524biological_processnegative regulation of neuron apoptotic process
A0045471biological_processresponse to ethanol
A0046620biological_processregulation of organ growth
A0046688biological_processresponse to copper ion
A0046716biological_processmuscle cell cellular homeostasis
A0046872molecular_functionmetal ion binding
A0048538biological_processthymus development
A0048678biological_processresponse to axon injury
A0050665biological_processhydrogen peroxide biosynthetic process
A0050728biological_processnegative regulation of inflammatory response
A0050766biological_processpositive regulation of phagocytosis
A0051087molecular_functionprotein-folding chaperone binding
A0051881biological_processregulation of mitochondrial membrane potential
A0060047biological_processheart contraction
A0060052biological_processneurofilament cytoskeleton organization
A0060087biological_processrelaxation of vascular associated smooth muscle
A0060088biological_processauditory receptor cell stereocilium organization
A0070062cellular_componentextracellular exosome
A0071276biological_processcellular response to cadmium ion
A0071318biological_processcellular response to ATP
A0072593biological_processreactive oxygen species metabolic process
A0097332biological_processresponse to antipsychotic drug
A1902177biological_processpositive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A1904115cellular_componentaxon cytoplasm
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 154
ChainResidue
AHIS71
AHIS80
AASP83
AHIS63
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 A 155
ChainResidue
AHIS46
AHIS48
AHIS63
AHIS120
site_idCU
Number of Residues4
DetailsREDUCED COPPER ION (CU1+) IS COORDINATED BY THREE HISTIDINES: HIS 46, METAL COORDINATED THROUGH ND1; HIS 48, METAL COORDINATED THROUGH NE2; HIS 120 METAL COORDINATED THROUGH NE2. THE THREE MENTIONED HISTIDINES ARE PROTONATED ON THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 46 IS HIS-E, HIS 48 IS HIS-D, HIS 120 IS HIS-D. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE ABOVE FINDINGS.
ChainResidue
AHIS46
AHIS48
AHIS120
ACU1155
site_idZN
Number of Residues4
DetailsZINC ION (ZN2+) IS COORDINATED BY THREE HISTIDINES AND BY AN ASPARTIC ACID RESIDUE. HIS 63, HIS 71 AND HIS 80 ARE METAL COORDINATED THROUGH THE ND1 ATOM. ASP 83 IS METAL COORDINATED THROUGH OD1. THE THREE HISTIDINES COORDINATED TO THE ZN ION ARE PROTONATED AT THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 63, HIS 71 AND HIS 80 ARE ALL HIS-E. THERE ARE DIRECT SPECTROSCOPIC EVIDENCES FOR THE COORDINATION AND PROTONATION PROPERTIES OF THE HIS RESIDUES. IN ADDITION, THERE ARE SPECTROSCOPIC EVIDENCES THAT THE NON METAL COORDINATED RESIDUE HIS 43 IS PROTONATED ON BOTH N IMIDAZOLE POSITION, I.E. HIS 43 IS HIS-H.
ChainResidue
AHIS63
AHIS71
AHIS80
AZN154
Functional Information from PROSITE/UniProt
site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI
ChainResidueDetails
AGLY138-ILE149
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12963370","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17548825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20727846","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07632","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"24140062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"22496122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)","evidences":[{"source":"PubMed","id":"20600836","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AARG143
AHIS63
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS63

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PDB entries from 2025-12-24

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