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6E8F

Crystal Structure of Human Protocadherin-15 EC3-5 CD2-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
A0016020cellular_componentmembrane
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
B0016020cellular_componentmembrane
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 701
ChainResidue
AASN368
AGLN370
AASP409
AASP411
AASP471

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 702
ChainResidue
AASP490
AASP523
AGLU385
AGLU458
AASP487
AALA488

site_idAC3
Number of Residues4
Detailsbinding site for residue CA A 703
ChainResidue
AGLU385
AASP456
AGLU458
AASP490

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 704
ChainResidue
AASN489
AASN491
AASP521
AASP523
AASN527
AASP573

site_idAC5
Number of Residues4
Detailsbinding site for residue NA A 705
ChainResidue
AASP366
AGLU367
AASN369
AASP411

site_idAC6
Number of Residues7
Detailsbinding site for residue CA C 701
ChainResidue
CASN368
CGLN370
CASP409
CASP411
CASP471
CGLN474
CHOH802

site_idAC7
Number of Residues6
Detailsbinding site for residue CA C 702
ChainResidue
CGLU385
CGLU458
CASP487
CALA488
CASP490
CASP523

site_idAC8
Number of Residues6
Detailsbinding site for residue CA C 703
ChainResidue
CASN489
CASN491
CASP521
CASP523
CASN527
CASP573

site_idAC9
Number of Residues4
Detailsbinding site for residue CA C 704
ChainResidue
CGLU385
CASP456
CGLU458
CASP490

site_idAD1
Number of Residues5
Detailsbinding site for residue CA B 701
ChainResidue
BASN368
BGLN370
BASP409
BASP411
BASP471

site_idAD2
Number of Residues6
Detailsbinding site for residue CA B 702
ChainResidue
BGLU385
BGLU458
BASP487
BALA488
BASP490
BASP523

site_idAD3
Number of Residues4
Detailsbinding site for residue CA B 703
ChainResidue
BGLU385
BASP456
BGLU458
BASP490

site_idAD4
Number of Residues6
Detailsbinding site for residue CA B 704
ChainResidue
BASN489
BASN491
BASP521
BASP523
BASN527
BASP573

site_idAD5
Number of Residues4
Detailsbinding site for residue CA B 705
ChainResidue
BASP366
BGLU367
BASN369
BASP411

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IqVmDaNDNtP
ChainResidueDetails
AILE483-PRO493

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN398
AASN545
CASN398
CASN545
BASN398
BASN545

221051

PDB entries from 2024-06-12

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