Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6VEL

Crystal Structure of Human E-cadherin bound by mouse monoclonal antibody 66E8Fab

Functional Information from GO Data
ChainGOidnamespacecontents
C0000794cellular_componentcondensed nuclear chromosome
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005886cellular_componentplasma membrane
C0005940cellular_componentseptin ring
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
C0016020cellular_componentmembrane
C0016925biological_processprotein sumoylation
C0031386molecular_functionprotein tag activity
C0042802molecular_functionidentical protein binding
C0044389molecular_functionubiquitin-like protein ligase binding
C0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 H 301
ChainResidue
CSO4404
HGLY118
HASN119
HTYR120
HTYR121

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 H 302
ChainResidue
HTYR121
LTYR51
LHIS110
CLYS206
CSER303
CTHR304
HTYR120

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 L 301
ChainResidue
CGLY301
LGLU112
LTYR113
LHOH403
LHOH407
LHOH433

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 L 302
ChainResidue
LGLN56
LLYS64
LPHE81
LGLU100
LASP101

site_idAC5
Number of Residues5
Detailsbinding site for residue CA C 401
ChainResidue
CGLU112
CASP168
CGLU170
CASP204
CHOH503

site_idAC6
Number of Residues6
Detailsbinding site for residue CA C 402
ChainResidue
CASN203
CASN205
CASP235
CASP237
CASN244
CASP296

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 C 403
ChainResidue
CVAL104
CVAL104
CILE105
CILE105
CMET193
CMET193
CHOH511

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 C 404
ChainResidue
CTHR305
HGLY50
HSO4301

site_idAC9
Number of Residues6
Detailsbinding site for residue CA C 405
ChainResidue
CGLU112
CGLU170
CASP201
CGLN202
CASP204
CASP237

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR211-HIS217

site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. ItVtDqNDNkP
ChainResidueDetails
CILE197-PRO207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950
ChainResidueDetails
CSER5

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
CSER7

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
CGLY101

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
CASP235
CASP204

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by S.pyogenes SpeB => ECO:0000269|PubMed:23532847
ChainResidueDetails
CTHR311

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000250|UniProtKB:P09803
ChainResidueDetails
CSER227

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) threonine => ECO:0000250|UniProtKB:P09803
ChainResidueDetails
CTHR232
CTHR305

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon