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3PMR

Crystal Structure of E2 domain of Human Amyloid Precursor-Like Protein 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 2
ChainResidue
AHOH24
AHOH173
ALYS484
AARG487
AARG491

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 3
ChainResidue
AARG431
BGLN494
BHIS495
AHOH92
AHOH156
AHOH207
AGLU380

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1
ChainResidue
AGLN494
AHIS495
BGLU380
BARG431

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 4
ChainResidue
BHOH19
BHOH52
BHOH109
BLYS484
BARG487
BARG491

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues382
DetailsDomain: {"description":"E2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01218","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues126
DetailsRegion: {"description":"Heparin-binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsRegion: {"description":"Collagen-binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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