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6FN8

Domain II of the HUMAN COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE at 1.55 A resolution

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS147
AHIS155
AHIS164
AASP167

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS147
BHIS155
BHIS164
BASP167

Functional Information from PROSITE/UniProt
site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNSGeRlACgiI
ChainResidueDetails
AGLY219-ILE230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues292
DetailsRegion: {"description":"Superoxide dismutase-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10677207","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DO5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"20154138","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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