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5DCX

Structural studies of AAV2 Rep68 reveal a partially structured linker and compact domain conformation

Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG A 301
ChainResidue
AGLU83
AHIS90
AHIS92

site_idAC2
Number of Residues3
Detailsbinding site for residue MG B 301
ChainResidue
BGLU83
BHIS90
BHIS92

site_idAC3
Number of Residues3
Detailsbinding site for residue MG C 301
ChainResidue
CGLU83
CHIS90
CHIS92

site_idAC4
Number of Residues3
Detailsbinding site for residue MG D 301
ChainResidue
DGLU83
DHIS90
DHIS92

site_idAC5
Number of Residues4
Detailsbinding site for residue MG E 301
ChainResidue
EGLU83
EHIS90
EHIS92
EHOH410

site_idAC6
Number of Residues3
Detailsbinding site for residue MG F 301
ChainResidue
FGLU83
FHIS90
FHIS92

site_idAC7
Number of Residues3
Detailsbinding site for residue MG G 301
ChainResidue
GGLU83
GHIS90
GHIS92

site_idAC8
Number of Residues3
Detailsbinding site for residue MG H 301
ChainResidue
HGLU83
HHIS90
HHIS92

site_idAC9
Number of Residues3
Detailsbinding site for residue MG I 301
ChainResidue
IGLU83
IHIS90
IHIS92

site_idAD1
Number of Residues3
Detailsbinding site for residue MG J 301
ChainResidue
JGLU83
JHIS90
JHIS92

site_idAD2
Number of Residues3
Detailsbinding site for residue MG K 301
ChainResidue
KGLU83
KHIS90
KHIS92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues11
DetailsACT_SITE: For nuclease activity => ECO:0000255|PROSITE-ProRule:PRU01366
ChainResidueDetails
ATYR156
JTYR156
KTYR156
BTYR156
CTYR156
DTYR156
ETYR156
FTYR156
GTYR156
HTYR156
ITYR156

site_idSWS_FT_FI2
Number of Residues33
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01366
ChainResidueDetails
AGLU83
DGLU83
DHIS90
DHIS92
EGLU83
EHIS90
EHIS92
FGLU83
FHIS90
FHIS92
GGLU83
AHIS90
GHIS90
GHIS92
HGLU83
HHIS90
HHIS92
IGLU83
IHIS90
IHIS92
JGLU83
JHIS90
AHIS92
JHIS92
KGLU83
KHIS90
KHIS92
BGLU83
BHIS90
BHIS92
CGLU83
CHIS90
CHIS92

222415

PDB entries from 2024-07-10

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