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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 Residues1288
DetailsDomain: {"description":"E1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues760
DetailsRegion: {"description":"GFLD subdomain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues464
DetailsRegion: {"description":"CuBD subdomain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues112
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8158260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17239395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25122912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2FK1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17239395","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2FK1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8344894","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsSite: {"description":"Required for Cu(2+) reduction","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsSite: {"description":"Cleavage; by caspases","evidences":[{"source":"PubMed","id":"10319819","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"8999878","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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