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3GTV

Human-mouse SOD1 chimera

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0006801biological_processsuperoxide metabolic process
A0046872molecular_functionmetal ion binding
B0005507molecular_functioncopper ion binding
B0006801biological_processsuperoxide metabolic process
B0046872molecular_functionmetal ion binding
C0005507molecular_functioncopper ion binding
C0006801biological_processsuperoxide metabolic process
C0046872molecular_functionmetal ion binding
D0005507molecular_functioncopper ion binding
D0006801biological_processsuperoxide metabolic process
D0046872molecular_functionmetal ion binding
E0005507molecular_functioncopper ion binding
E0006801biological_processsuperoxide metabolic process
E0046872molecular_functionmetal ion binding
F0005507molecular_functioncopper ion binding
F0006801biological_processsuperoxide metabolic process
F0046872molecular_functionmetal ion binding
G0005507molecular_functioncopper ion binding
G0006801biological_processsuperoxide metabolic process
G0046872molecular_functionmetal ion binding
H0005507molecular_functioncopper ion binding
H0006801biological_processsuperoxide metabolic process
H0046872molecular_functionmetal ion binding
I0005507molecular_functioncopper ion binding
I0006801biological_processsuperoxide metabolic process
I0046872molecular_functionmetal ion binding
J0005507molecular_functioncopper ion binding
J0006801biological_processsuperoxide metabolic process
J0046872molecular_functionmetal ion binding
K0005507molecular_functioncopper ion binding
K0006801biological_processsuperoxide metabolic process
K0046872molecular_functionmetal ion binding
L0005507molecular_functioncopper ion binding
L0006801biological_processsuperoxide metabolic process
L0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 155
ChainResidue
AHIS63
AHIS71
AHIS80
AASP83

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 155
ChainResidue
BHIS63
BHIS71
BHIS80
BASP83

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 155
ChainResidue
CHIS71
CHIS80
CASP83
CHIS63

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 155
ChainResidue
DHIS63
DHIS71
DHIS80
DASP83

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 155
ChainResidue
EHIS63
EHIS71
EHIS80
EASP83
ELYS136

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN F 155
ChainResidue
FHIS63
FHIS71
FHIS80
FASP83
FLYS136

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 155
ChainResidue
GHIS63
GHIS71
GHIS80
GASP83

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 155
ChainResidue
HHIS63
HHIS71
HHIS80
HASP83

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN I 155
ChainResidue
IHIS63
IHIS71
IHIS80
IASP83

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN J 155
ChainResidue
JHIS63
JHIS71
JHIS80
JASP83

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN K 155
ChainResidue
KHIS63
KHIS71
KHIS80
KASP83

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN L 155
ChainResidue
LHIS63
LHIS71
LHIS80
LASP83

Functional Information from PROSITE/UniProt
site_idPS00087
Number of Residues11
DetailsSOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEfGDnT
ChainResidueDetails
AGLY44-THR54

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 Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
ChainResidueDetails
AHIS46
AHIS48
BHIS46
BHIS48
CHIS46
CHIS48
DHIS46
DHIS48
EHIS46
EHIS48
FHIS46
FHIS48
GHIS46
GHIS48
HHIS46
HHIS48
IHIS46
IHIS48
JHIS46
JHIS48
KHIS46
KHIS48
LHIS46
LHIS48

site_idSWS_FT_FI2
Number of Residues48
DetailsBINDING: BINDING => ECO:0000269|PubMed:20727846
ChainResidueDetails
AHIS63
AHIS71
AHIS80
JHIS63
JHIS71
JHIS80
JASP83
KHIS63
KHIS71
KHIS80
KASP83
LHIS63
LHIS71
LHIS80
LASP83
AASP83
BHIS63
BHIS71
BHIS80
BASP83
CHIS63
CHIS71
CHIS80
CASP83
DHIS63
DHIS71
DHIS80
DASP83
EHIS63
EHIS71
EHIS80
EASP83
FHIS63
FHIS71
FHIS80
FASP83
GHIS63
GHIS71
GHIS80
GASP83
HHIS63
HHIS71
HHIS80
HASP83
IHIS63
IHIS71
IHIS80
IASP83

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA1
BALA1
CALA1
DALA1
EALA1
FALA1
GALA1
HALA1
IALA1
JALA1
KALA1
LALA1

site_idSWS_FT_FI4
Number of Residues24
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P08228
ChainResidueDetails
GLYS3
GLYS9
HLYS3
HLYS9
ILYS3
ILYS9
JLYS3
JLYS9
KLYS3
KLYS9
LLYS3
LLYS9
ALYS3
ALYS9
BLYS3
BLYS9
CLYS3
CLYS9
DLYS3
DLYS9
ELYS3
ELYS9
FLYS3
FLYS9

site_idSWS_FT_FI5
Number of Residues12
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
ChainResidueDetails
ACYS6
BCYS6
CCYS6
DCYS6
ECYS6
FCYS6
GCYS6
HCYS6
ICYS6
JCYS6
KCYS6
LCYS6

site_idSWS_FT_FI6
Number of Residues24
DetailsCROSSLNK: 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
ChainResidueDetails
GTRP32
HTRP32
ITRP32
JTRP32
KTRP32
LTRP32
ATRP32
BTRP32
CTRP32
DTRP32
ETRP32
FTRP32

site_idSWS_FT_FI7
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BHIS120
DHIS120
FHIS120
HHIS120
JHIS120
LHIS120
AHIS120
CHIS120
EHIS120
GHIS120
IHIS120
KHIS120

site_idSWS_FT_FI8
Number of Residues12
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS91
BLYS91
CLYS91
DLYS91
ELYS91
FLYS91
GLYS91
HLYS91
ILYS91
JLYS91
KLYS91
LLYS91

site_idSWS_FT_FI9
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00441
ChainResidueDetails
ASER98
BSER98
CSER98
DSER98
ESER98
FSER98
GSER98
HSER98
ISER98
JSER98
KSER98
LSER98

site_idSWS_FT_FI10
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07632
ChainResidueDetails
ASER105
BSER105
CSER105
DSER105
ESER105
FSER105
GSER105
HSER105
ISER105
JSER105
KSER105
LSER105

site_idSWS_FT_FI11
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER107
BSER107
CSER107
DSER107
ESER107
FSER107
GSER107
HSER107
ISER107
JSER107
KSER107
LSER107

site_idSWS_FT_FI12
Number of Residues24
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
GLYS122
GLYS136
HLYS122
HLYS136
ILYS122
ILYS136
JLYS122
JLYS136
KLYS122
KLYS136
LLYS122
LLYS136
ALYS122
ALYS136
BLYS122
BLYS136
CLYS122
CLYS136
DLYS122
DLYS136
ELYS122
ELYS136
FLYS122
FLYS136

219869

PDB entries from 2024-05-15

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