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3KTM

Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008201molecular_functionheparin binding
A0016020cellular_componentmembrane
A0046914molecular_functiontransition metal ion binding
B0008201molecular_functionheparin binding
B0016020cellular_componentmembrane
B0046914molecular_functiontransition metal ion binding
C0008201molecular_functionheparin binding
C0016020cellular_componentmembrane
C0046914molecular_functiontransition metal ion binding
D0008201molecular_functionheparin binding
D0016020cellular_componentmembrane
D0046914molecular_functiontransition metal ion binding
E0008201molecular_functionheparin binding
E0016020cellular_componentmembrane
E0046914molecular_functiontransition metal ion binding
F0008201molecular_functionheparin binding
F0016020cellular_componentmembrane
F0046914molecular_functiontransition metal ion binding
G0008201molecular_functionheparin binding
G0016020cellular_componentmembrane
G0046914molecular_functiontransition metal ion binding
H0008201molecular_functionheparin binding
H0016020cellular_componentmembrane
H0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BU4 A 1
ChainResidue
ATHR83
AASN84
APRO173
ACYS174
AGLY175
AILE176

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BU4 B 7
ChainResidue
GARG194
BPRO188
BLEU189
BALA190

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 2
ChainResidue
BALA88
BASN89
BARG116
BHOH209
BHOH221
BHOH226
HARG194

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 208
ChainResidue
BGLN90
BHIS151
BLYS155
HACT6

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BU4 C 5
ChainResidue
AARG194
CLEU189
CALA190

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 3
ChainResidue
CASN89
CARG116
CHOH210
CHOH216
EARG194

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 8
ChainResidue
CGLN90
CHIS151
EACT9
ELYS155

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BU4 D 2
ChainResidue
DTHR83
DASN84
DPRO173
DCYS174
DGLY175

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 5
ChainResidue
AARG180
DARG140
FHOH5

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BU4 E 6
ChainResidue
ELEU189
EALA190
FARG194

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 E 4
ChainResidue
CARG194
EALA88
EASN89
EARG116
EHOH210
EHOH231

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT E 9
ChainResidue
CACT8
EGLN90
EHIS151
ELYS155

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BU4 F 4
ChainResidue
FGLY175
FILE176

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BU4 G 3
ChainResidue
GPRO173
GCYS174
GGLY175
GILE176

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BU4 H 8
ChainResidue
DARG194
HLEU189
HALA190

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 H 1
ChainResidue
BARG194
HALA88
HASN89
HARG116
HHOH227
HHOH228
HHOH230
HHOH246

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT H 6
ChainResidue
BACT208
HGLN90
HHIS151
HLYS155

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 Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:8158260
ChainResidueDetails
AASN96
BASN96
CASN96
DASN96
EASN96
FASN96
GASN96
HASN96

site_idSWS_FT_FI2
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_FI3
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_FI4
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_FI5
Number of Residues8
DetailsSITE: Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217
ChainResidueDetails
AMET170
BMET170
CMET170
DMET170
EMET170
FMET170
GMET170
HMET170

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PDB entries from 2024-07-31

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