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6N2E

Crystal Structure of Human Protocadherin-15 EC1-3 G16D N369D Q370N and Mouse Cadherin-23 EC1-2 T15E

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
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
B0007605biological_processsensory perception of sound
B0016020cellular_componentmembrane
B0032420cellular_componentstereocilium
B0048839biological_processinner ear development
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
C0016020cellular_componentmembrane
C0098609biological_processcell-cell adhesion
D0005509molecular_functioncalcium ion binding
D0005886cellular_componentplasma membrane
D0007155biological_processcell adhesion
D0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
D0016020cellular_componentmembrane
D0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 401
ChainResidue
AGLU27
AGLU28
AASP83
AASP85
AASP121

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AASP121
AASP159
AGLU27
AASP85
AASP118
AARG119

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

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 404
ChainResidue
AGLU137
AASP236
AGLY237
AASP239
AASP289
AHOH513

site_idAC5
Number of Residues5
Detailsbinding site for residue CA A 405
ChainResidue
AASP238
ALEU240
AASP287
AASP289
AGLN348

site_idAC6
Number of Residues6
Detailsbinding site for residue CA B 401
ChainResidue
BGLU27
BGLU28
BASP83
BASP85
BASP121
BHOH518

site_idAC7
Number of Residues6
Detailsbinding site for residue CA B 402
ChainResidue
BGLU27
BASP85
BASP118
BARG119
BASP121
BASP159

site_idAC8
Number of Residues6
Detailsbinding site for residue CA B 403
ChainResidue
BASN120
BASN122
BASP157
BASP159
BASN163
BASP215

site_idAC9
Number of Residues5
Detailsbinding site for residue CA B 404
ChainResidue
BASP238
BLEU240
BASP287
BASP289
BGLN348

site_idAD1
Number of Residues6
Detailsbinding site for residue CA B 405
ChainResidue
BGLU137
BASP236
BGLY237
BASP239
BASP289
BHOH513

site_idAD2
Number of Residues6
Detailsbinding site for residue CA C 301
ChainResidue
CASN103
CASN105
CASP135
CASP137
CGLY141
CASP186

site_idAD3
Number of Residues5
Detailsbinding site for residue CA C 302
ChainResidue
CGLU21
CASP71
CGLU73
CASP104
CHOH401

site_idAD4
Number of Residues6
Detailsbinding site for residue CA C 303
ChainResidue
CGLU21
CGLU73
CASP101
CVAL102
CASP104
CASP137

site_idAD5
Number of Residues6
Detailsbinding site for residue CA C 304
ChainResidue
CASN3
CARG4
CASP36
CASP38
CASP40
CASP86

site_idAD6
Number of Residues6
Detailsbinding site for residue CA D 301
ChainResidue
DASN103
DASN105
DASP135
DASP137
DGLY141
DASP186

site_idAD7
Number of Residues6
Detailsbinding site for residue CA D 302
ChainResidue
DGLU21
DGLU73
DASP101
DVAL102
DASP104
DASP137

site_idAD8
Number of Residues5
Detailsbinding site for residue CA D 303
ChainResidue
DGLU21
DASP71
DGLU73
DASP104
DHOH401

site_idAD9
Number of Residues6
Detailsbinding site for residue CA D 304
ChainResidue
DASP36
DASP38
DASP40
DASP86
DASN3
DARG4

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IqVgDvNDNaP
ChainResidueDetails
CILE97-PRO107
AILE114-PRO124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN31
AASN76
AASN180
BASN31
BASN76
BASN180

221051

PDB entries from 2024-06-12

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