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1BA9

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0000303biological_processresponse to superoxide
A0001541biological_processovarian follicle development
A0001819biological_processpositive regulation of cytokine production
A0001890biological_processplacenta development
A0001895biological_processretina homeostasis
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
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006749biological_processglutathione metabolic process
A0006801biological_processsuperoxide metabolic process
A0006879biological_processintracellular iron ion homeostasis
A0006915biological_processapoptotic process
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
A0008340biological_processdetermination of adult lifespan
A0009408biological_processresponse to heat
A0009410biological_processresponse to xenobiotic stimulus
A0010033biological_processresponse to organic substance
A0010467biological_processgene expression
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019226biological_processtransmission of nerve impulse
A0019228biological_processneuronal action potential
A0019430biological_processremoval of superoxide radicals
A0030346molecular_functionprotein phosphatase 2B binding
A0031267molecular_functionsmall GTPase binding
A0031410cellular_componentcytoplasmic vesicle
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
A0035234biological_processectopic germ cell programmed cell death
A0040014biological_processregulation of multicellular organism growth
A0042542biological_processresponse to hydrogen peroxide
A0042554biological_processsuperoxide anion generation
A0042802molecular_functionidentical protein binding
A0043025cellular_componentneuronal cell body
A0043065biological_processpositive regulation of apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0043085biological_processpositive regulation of catalytic activity
A0043087biological_processregulation of GTPase activity
A0043410biological_processpositive regulation of MAPK cascade
A0043524biological_processnegative regulation of neuron apoptotic process
A0045471biological_processresponse to ethanol
A0045541biological_processnegative regulation of cholesterol biosynthetic process
A0045859biological_processregulation of protein kinase activity
A0046620biological_processregulation of organ growth
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
A0051093biological_processnegative regulation of developmental process
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
A0072593biological_processreactive oxygen species metabolic process
A0099610biological_processaction potential initiation
A1902177biological_processpositive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A1904115cellular_componentaxon cytoplasm
A2000242biological_processnegative regulation of reproductive process
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: BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
ChainResidueDetails
AVAL47
AGLU49
AGLU121

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20727846
ChainResidueDetails
APHE64
AGLY72
AVAL81
ALEU84

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
ChainResidueDetails
ATHR2

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P08228
ChainResidueDetails
AALA4
AGLY10
AASP92

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
AILE99

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AVAL103

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07632
ChainResidueDetails
ALEU106

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P08228
ChainResidueDetails
AGLY108

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
ChainResidueDetails
AALA123

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
ChainResidueDetails
ATHR137

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
ChainResidueDetails
AVAL7

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
ChainResidueDetails
AGLY33

218853

PDB entries from 2024-04-24

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