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5X7Y

Crystal Structure of the Dog Lipocalin Allergen Can f 6

Functional Information from GO Data
ChainGOidnamespacecontents
A0005549molecular_functionodorant binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0036094molecular_functionsmall molecule binding
B0005549molecular_functionodorant binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0036094molecular_functionsmall molecule binding
C0005549molecular_functionodorant binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0036094molecular_functionsmall molecule binding
D0005549molecular_functionodorant binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0036094molecular_functionsmall molecule binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue PEG A 201
ChainResidue
AMET40
AVAL42
APHE57
ALEU108
AGLU121

site_idAC2
Number of Residues3
Detailsbinding site for residue PEG B 201
ChainResidue
BMET40
BVAL42
BGLU121

site_idAC3
Number of Residues4
Detailsbinding site for residue PEG C 201
ChainResidue
CVAL42
CPHE57
CGLU121
CMET40

site_idAC4
Number of Residues4
Detailsbinding site for residue PEG D 201
ChainResidue
DMET40
DVAL42
DGLU121
DTYR123

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFDisKISGDWYSI
ChainResidueDetails
AASN11-ILE24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN37
DASN37
DASN52
DASN75
AASN52
AASN75
BASN37
BASN52
BASN75
CASN37
CASN52
CASN75

218853

PDB entries from 2024-04-24

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