3KTM
Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008201 | molecular_function | heparin binding |
| A | 0016020 | cellular_component | membrane |
| A | 0046914 | molecular_function | transition metal ion binding |
| B | 0008201 | molecular_function | heparin binding |
| B | 0016020 | cellular_component | membrane |
| B | 0046914 | molecular_function | transition metal ion binding |
| C | 0008201 | molecular_function | heparin binding |
| C | 0016020 | cellular_component | membrane |
| C | 0046914 | molecular_function | transition metal ion binding |
| D | 0008201 | molecular_function | heparin binding |
| D | 0016020 | cellular_component | membrane |
| D | 0046914 | molecular_function | transition metal ion binding |
| E | 0008201 | molecular_function | heparin binding |
| E | 0016020 | cellular_component | membrane |
| E | 0046914 | molecular_function | transition metal ion binding |
| F | 0008201 | molecular_function | heparin binding |
| F | 0016020 | cellular_component | membrane |
| F | 0046914 | molecular_function | transition metal ion binding |
| G | 0008201 | molecular_function | heparin binding |
| G | 0016020 | cellular_component | membrane |
| G | 0046914 | molecular_function | transition metal ion binding |
| H | 0008201 | molecular_function | heparin binding |
| H | 0016020 | cellular_component | membrane |
| H | 0046914 | molecular_function | transition metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BU4 A 1 |
| Chain | Residue |
| A | THR83 |
| A | ASN84 |
| A | PRO173 |
| A | CYS174 |
| A | GLY175 |
| A | ILE176 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BU4 B 7 |
| Chain | Residue |
| G | ARG194 |
| B | PRO188 |
| B | LEU189 |
| B | ALA190 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2 |
| Chain | Residue |
| B | ALA88 |
| B | ASN89 |
| B | ARG116 |
| B | HOH209 |
| B | HOH221 |
| B | HOH226 |
| H | ARG194 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 208 |
| Chain | Residue |
| B | GLN90 |
| B | HIS151 |
| B | LYS155 |
| H | ACT6 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BU4 C 5 |
| Chain | Residue |
| A | ARG194 |
| C | LEU189 |
| C | ALA190 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3 |
| Chain | Residue |
| C | ASN89 |
| C | ARG116 |
| C | HOH210 |
| C | HOH216 |
| E | ARG194 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 8 |
| Chain | Residue |
| C | GLN90 |
| C | HIS151 |
| E | ACT9 |
| E | LYS155 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BU4 D 2 |
| Chain | Residue |
| D | THR83 |
| D | ASN84 |
| D | PRO173 |
| D | CYS174 |
| D | GLY175 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 5 |
| Chain | Residue |
| A | ARG180 |
| D | ARG140 |
| F | HOH5 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BU4 E 6 |
| Chain | Residue |
| E | LEU189 |
| E | ALA190 |
| F | ARG194 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 E 4 |
| Chain | Residue |
| C | ARG194 |
| E | ALA88 |
| E | ASN89 |
| E | ARG116 |
| E | HOH210 |
| E | HOH231 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT E 9 |
| Chain | Residue |
| C | ACT8 |
| E | GLN90 |
| E | HIS151 |
| E | LYS155 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BU4 F 4 |
| Chain | Residue |
| F | GLY175 |
| F | ILE176 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BU4 G 3 |
| Chain | Residue |
| G | PRO173 |
| G | CYS174 |
| G | GLY175 |
| G | ILE176 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BU4 H 8 |
| Chain | Residue |
| D | ARG194 |
| H | LEU189 |
| H | ALA190 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 H 1 |
| Chain | Residue |
| B | ARG194 |
| H | ALA88 |
| H | ASN89 |
| H | ARG116 |
| H | HOH227 |
| H | HOH228 |
| H | HOH230 |
| H | HOH246 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT H 6 |
| Chain | Residue |
| B | ACT208 |
| H | GLN90 |
| H | HIS151 |
| H | LYS155 |
Functional Information from PROSITE/UniProt
| site_id | PS00319 |
| Number of Residues | 8 |
| Details | APP_CUBD Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. GVEFVCCP |
| Chain | Residue | Details |
| A | GLY181-PRO188 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1288 |
| Details | Domain: {"description":"E1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 760 |
| Details | Region: {"description":"GFLD subdomain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 464 |
| Details | Region: {"description":"CuBD subdomain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 112 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8158260","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17239395","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2FK1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8344894","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Site: {"description":"Required for Cu(2+) reduction","evidences":[{"source":"PROSITE-ProRule","id":"PRU01217","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Site: {"description":"Cleavage; by caspases","evidences":[{"source":"PubMed","id":"10319819","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"PubMed","id":"8999878","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






