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2FK3

Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0046914molecular_functiontransition metal ion binding
B0016020cellular_componentmembrane
B0046914molecular_functiontransition metal ion binding
C0016020cellular_componentmembrane
C0046914molecular_functiontransition metal ion binding
D0016020cellular_componentmembrane
D0046914molecular_functiontransition metal ion binding
E0016020cellular_componentmembrane
E0046914molecular_functiontransition metal ion binding
F0016020cellular_componentmembrane
F0046914molecular_functiontransition metal ion binding
G0016020cellular_componentmembrane
G0046914molecular_functiontransition metal ion binding
H0016020cellular_componentmembrane
H0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU C 201
ChainResidue
CHIS137
GHIS137
GHOH190

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU C 202
ChainResidue
CGLU131
HHIS137
HGLU139

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CU B 203
ChainResidue
BHIS137
DHIS137

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 204
ChainResidue
AGLU139
AHOH237
GGLU131
AHIS137

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU E 205
ChainResidue
DGLU131
EHIS137
EGLU139
EHOH238

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU F 206
ChainResidue
BGLU131
FHIS137
FGLU139

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU H 207
ChainResidue
EHOH224
EHOH225
EHOH226
HHOH212
HHOH213
HHOH214

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 208
ChainResidue
AHOH214
AHOH217
AHOH218
FHOH220
FHOH221

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU H 209
ChainResidue
HHOH223
HHOH224
HHOH231
HHOH232

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CU C 210
ChainResidue
CHOH244

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 211
ChainResidue
AHOH235
AHOH236
AHOH237

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU E 212
ChainResidue
ELEU165
EHIS166
HLEU165
HHIS166
HHOH213

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 213
ChainResidue
ALEU165
AHIS166
FLEU165
FHIS166

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CU B 214
ChainResidue
BTYR168
CTYR168

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 215
ChainResidue
DTYR168
DHOH229
GTYR168
GHOH209

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CU D 216
ChainResidue
EHOH221

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU F 217
ChainResidue
FSER159
FTHR163
FASN164
FHOH222

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CU F 219
ChainResidue
AHOH227

Functional Information from PROSITE/UniProt
site_idPS00319
Number of Residues8
DetailsAPP_CUBD Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. GVEFVCCP
ChainResidueDetails
AGLY181-PRO188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1
ChainResidueDetails
AHIS147
EHIS151
FHIS147
FHIS151
GHIS147
GHIS151
HHIS147
HHIS151
AHIS151
BHIS147
BHIS151
CHIS147
CHIS151
DHIS147
DHIS151
EHIS147

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1
ChainResidueDetails
ATYR168
BTYR168
CTYR168
DTYR168
ETYR168
FTYR168
GTYR168
HTYR168

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000305|PubMed:8344894
ChainResidueDetails
AGLU183
DGLU183
DCYS186
DCYS187
EGLU183
ECYS186
ECYS187
FGLU183
FCYS186
FCYS187
GGLU183
ACYS186
GCYS186
GCYS187
HGLU183
HCYS186
HCYS187
ACYS187
BGLU183
BCYS186
BCYS187
CGLU183
CCYS186
CCYS187

site_idSWS_FT_FI4
Number of Residues8
DetailsSITE: Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217
ChainResidueDetails
AMET170
BMET170
CMET170
DMET170
EMET170
FMET170
GMET170
HMET170

220113

PDB entries from 2024-05-22

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