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4ZMT

Crystal structure of human P-cadherin (ss-X-dimer-long)

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
A0098609biological_processcell-cell adhesion
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
B0016020cellular_componentmembrane
B0098609biological_processcell-cell adhesion
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
E0005509molecular_functioncalcium ion binding
E0005886cellular_componentplasma membrane
E0007155biological_processcell adhesion
E0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
E0016020cellular_componentmembrane
E0098609biological_processcell-cell adhesion
F0005509molecular_functioncalcium ion binding
F0005886cellular_componentplasma membrane
F0007155biological_processcell adhesion
F0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
F0016020cellular_componentmembrane
F0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 301
ChainResidue
AGLU11
AASP67
AGLU69
AASP103

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 302
ChainResidue
AASP136
AGLU11
AGLU69
AASP100
AGLN101
AASP103

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 303
ChainResidue
AASN102
AHIS104
AASP134
AASP136
AASN143
AASP195

site_idAC4
Number of Residues4
Detailsbinding site for residue CA B 301
ChainResidue
BGLU11
BASP67
BGLU69
BASP103

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 302
ChainResidue
BASN102
BHIS104
BASP134
BASP136
BASN143
BASP195

site_idAC6
Number of Residues6
Detailsbinding site for residue CA B 303
ChainResidue
BGLU11
BGLU69
BASP100
BGLN101
BASP103
BASP136

site_idAC7
Number of Residues6
Detailsbinding site for residue CA C 301
ChainResidue
CGLU11
CGLU69
CASP100
CGLN101
CASP103
CASP136

site_idAC8
Number of Residues6
Detailsbinding site for residue CA C 302
ChainResidue
CASN102
CHIS104
CASP134
CASP136
CASN143
CASP195

site_idAC9
Number of Residues4
Detailsbinding site for residue CA C 303
ChainResidue
CGLU11
CASP67
CGLU69
CASP103

site_idAD1
Number of Residues6
Detailsbinding site for residue CA D 301
ChainResidue
DASN102
DHIS104
DASP134
DASP136
DASN143
DASP195

site_idAD2
Number of Residues4
Detailsbinding site for residue CA D 302
ChainResidue
DGLU11
DASP67
DGLU69
DASP103

site_idAD3
Number of Residues6
Detailsbinding site for residue CA D 303
ChainResidue
DGLU11
DGLU69
DASP100
DGLN101
DASP103
DASP136

site_idAD4
Number of Residues4
Detailsbinding site for residue CA E 301
ChainResidue
EGLU11
EASP67
EGLU69
EASP103

site_idAD5
Number of Residues6
Detailsbinding site for residue CA E 302
ChainResidue
EGLU11
EGLU69
EASP100
EGLN101
EASP103
EASP136

site_idAD6
Number of Residues6
Detailsbinding site for residue CA E 303
ChainResidue
EASN102
EHIS104
EASP134
EASP136
EASN143
EASP195

site_idAD7
Number of Residues6
Detailsbinding site for residue CA F 301
ChainResidue
FGLU11
FGLU69
FASP100
FGLN101
FASP103
FASP136

site_idAD8
Number of Residues4
Detailsbinding site for residue CA F 302
ChainResidue
FGLU11
FASP67
FGLU69
FASP103

site_idAD9
Number of Residues6
Detailsbinding site for residue CA F 303
ChainResidue
FASN102
FHIS104
FASP134
FASP136
FASN143
FASP195

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IiVtDqNDHkP
ChainResidueDetails
AILE96-PRO106
AVAL209-PRO219

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN93
BASN93
CASN93
DASN93
EASN93
FASN93

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PDB entries from 2024-06-12

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