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3O79

Crystal Structure of Wild-type Rabbit PrP 126-230

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
B0016020cellular_componentmembrane
B0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 2
ChainResidue
AHOH55
AARG156
AASN197
AASP202

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 3
ChainResidue
AGLU152
AHOH11
AHOH36
AHOH90
AGLY142
AASP144

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1
ChainResidue
AARG136
AARG148

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 1
ChainResidue
BHOH44
BHOH94
BGLY142
BASP144
BGLU152
BHOH275

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 4
ChainResidue
AHOH79
AHOH91
BHOH19
BHOH31
BHOH96
BARG228

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 2
ChainResidue
BARG136
BARG148

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 231
ChainResidue
AARG164
AASP178
AASN181
BTYR128
BARG164
BHIS177
BASP178
BASN181

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 232
ChainResidue
BLEU138
BILE139
BHIS140
BASP147
BTYR150
BARG151

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 233
ChainResidue
AHOH17
ATYR145
BHOH12
BTYR226
BALA230

Functional Information from PROSITE/UniProt
site_idPS00706
Number of Residues19
DetailsPRION_2 Prion protein signature 2. EtDiKIMeRVVeQMCitQY
ChainResidueDetails
AGLU200-TYR218

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PDB entries from 2024-07-24

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