Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5CZR

Crystal Structure of Human Protocadherin-24 EC1-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell-cell adhesion
A0016020cellular_componentmembrane
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell-cell adhesion
B0016020cellular_componentmembrane
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell-cell adhesion
C0016020cellular_componentmembrane
D0005509molecular_functioncalcium ion binding
D0005886cellular_componentplasma membrane
D0007155biological_processcell adhesion
D0007156biological_processhomophilic cell-cell adhesion
D0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 1001
ChainResidue
AASN1
AVAL2
AASP32
AASP34
AASP36
AASP81

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 1002
ChainResidue
AASP99
AHOH1138
AHOH1154
AGLU17
AASP66
AGLU68

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 1003
ChainResidue
AGLU17
AGLU68
AASP96
AARG97
AASP99
AASP132

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 1004
ChainResidue
AASN98
AASN100
AASP130
AASP132
AALA136
AASP188

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 301
ChainResidue
BASN1
BVAL2
BASP32
BASP34
BASP36
BASP81

site_idAC6
Number of Residues6
Detailsbinding site for residue CA B 302
ChainResidue
BGLU17
BASP66
BGLU68
BASP99
BHOH441
BHOH447

site_idAC7
Number of Residues6
Detailsbinding site for residue CA B 303
ChainResidue
BGLU17
BGLU68
BASP96
BARG97
BASP99
BASP132

site_idAC8
Number of Residues6
Detailsbinding site for residue CA B 304
ChainResidue
BASN98
BASN100
BASP130
BASP132
BALA136
BASP188

site_idAC9
Number of Residues6
Detailsbinding site for residue CA C 301
ChainResidue
CASN1
CVAL2
CASP32
CASP34
CASP36
CASP81

site_idAD1
Number of Residues6
Detailsbinding site for residue CA C 302
ChainResidue
CGLU17
CASP66
CGLU68
CASP99
CHOH434
CHOH454

site_idAD2
Number of Residues6
Detailsbinding site for residue CA C 303
ChainResidue
CGLU17
CGLU68
CASP96
CARG97
CASP99
CASP132

site_idAD3
Number of Residues6
Detailsbinding site for residue CA C 304
ChainResidue
CASN98
CASN100
CASP130
CASP132
CALA136
CASP188

site_idAD4
Number of Residues6
Detailsbinding site for residue CA D 301
ChainResidue
DASN1
DVAL2
DASP32
DASP34
DASP36
DASP81

site_idAD5
Number of Residues6
Detailsbinding site for residue CA D 302
ChainResidue
DGLU17
DASP66
DGLU68
DASP99
DHOH427
DHOH432

site_idAD6
Number of Residues6
Detailsbinding site for residue CA D 303
ChainResidue
DGLU17
DGLU68
DASP96
DARG97
DASP99
DASP132

site_idAD7
Number of Residues6
Detailsbinding site for residue CA D 304
ChainResidue
DASN98
DASN100
DASP130
DASP132
DALA136
DASP188

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. ViVeDrNDNaP
ChainResidueDetails
AVAL92-PRO102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues388
DetailsDomain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon