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6MFO

Crystal Structure of Human Protocadherin-15 EC1-3 G16D N369D Q370N

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
A0007605biological_processsensory perception of sound
A0016020cellular_componentmembrane
A0032420cellular_componentstereocilium
A0048839biological_processinner ear development
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 401
ChainResidue
AGLU27
AGLU28
AASP83
AASP85
AASP121
AHOH501

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 402
ChainResidue
AARG119
AASP121
AASN122
AASP159
AGLU27
AASP85
AASP118

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
AASN120
AASN122
AASP157
AASP159
AASN163
AASP215

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 404
ChainResidue
AASP238
ALEU240
AASP287
AASP289
AGLN348

site_idAC5
Number of Residues5
Detailsbinding site for residue CA A 405
ChainResidue
AGLU137
AASP236
AGLY237
AASP239
AASP289

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IvVrDrNDNsP
ChainResidueDetails
AILE114-PRO124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN31
AASN76
AASN180

227111

PDB entries from 2024-11-06

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