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5F2Q

C-type lectin from Bothrops jararacussu

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0030246molecular_functioncarbohydrate binding
A0030308biological_processnegative regulation of cell growth
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0030246molecular_functioncarbohydrate binding
B0030308biological_processnegative regulation of cell growth
B0046872molecular_functionmetal ion binding
C0005576cellular_componentextracellular region
C0030246molecular_functioncarbohydrate binding
C0030308biological_processnegative regulation of cell growth
C0046872molecular_functionmetal ion binding
D0005576cellular_componentextracellular region
D0030246molecular_functioncarbohydrate binding
D0030308biological_processnegative regulation of cell growth
D0046872molecular_functionmetal ion binding
E0005576cellular_componentextracellular region
E0030246molecular_functioncarbohydrate binding
E0030308biological_processnegative regulation of cell growth
E0046872molecular_functionmetal ion binding
F0005576cellular_componentextracellular region
F0030246molecular_functioncarbohydrate binding
F0030308biological_processnegative regulation of cell growth
F0046872molecular_functionmetal ion binding
G0005576cellular_componentextracellular region
G0030246molecular_functioncarbohydrate binding
G0030308biological_processnegative regulation of cell growth
G0046872molecular_functionmetal ion binding
H0005576cellular_componentextracellular region
H0030246molecular_functioncarbohydrate binding
H0030308biological_processnegative regulation of cell growth
H0046872molecular_functionmetal ion binding
I0005576cellular_componentextracellular region
I0030246molecular_functioncarbohydrate binding
I0030308biological_processnegative regulation of cell growth
I0046872molecular_functionmetal ion binding
J0005576cellular_componentextracellular region
J0030246molecular_functioncarbohydrate binding
J0030308biological_processnegative regulation of cell growth
J0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue CA A 201
ChainResidue
AGLN96
AASP98
AGLU104
AASN119
AASP120
AHOH301
AHOH302

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 202
ChainResidue
AHIS44
AGLN132
ATYR15
ASER42

site_idAC3
Number of Residues6
Detailsbinding site for residue CA B 201
ChainResidue
BGLN96
BASP98
BGLU104
BASN119
BASP120
BHOH301

site_idAC4
Number of Residues5
Detailsbinding site for residue NA B 202
ChainResidue
BLEU13
BTYR15
BSER42
BHIS44
BGLN132

site_idAC5
Number of Residues5
Detailsbinding site for residue CA C 201
ChainResidue
CGLN96
CASP98
CGLU104
CASN119
CASP120

site_idAC6
Number of Residues4
Detailsbinding site for residue NA C 202
ChainResidue
CTYR15
CSER42
CHIS44
CGLN132

site_idAC7
Number of Residues6
Detailsbinding site for residue CA D 201
ChainResidue
DGLN96
DASP98
DGLU104
DASN119
DASP120
DHOH301

site_idAC8
Number of Residues4
Detailsbinding site for residue NA D 202
ChainResidue
DLEU13
DTYR15
DSER42
DGLN132

site_idAC9
Number of Residues6
Detailsbinding site for residue CA E 201
ChainResidue
EGLN96
EASP98
EGLU104
EASN119
EASP120
EHOH305

site_idAD1
Number of Residues6
Detailsbinding site for residue NA E 202
ChainResidue
ELEU13
ETYR15
ESER42
EGLN132
EHOH301
EHOH309

site_idAD2
Number of Residues6
Detailsbinding site for residue CA F 201
ChainResidue
FGLN96
FASP98
FGLU104
FASN119
FASP120
FHOH302

site_idAD3
Number of Residues4
Detailsbinding site for residue NA F 202
ChainResidue
FTYR15
FSER42
FGLN132
FHOH301

site_idAD4
Number of Residues6
Detailsbinding site for residue CA G 201
ChainResidue
GGLN96
GASP98
GGLU104
GASN119
GASP120
GHOH302

site_idAD5
Number of Residues4
Detailsbinding site for residue NA G 202
ChainResidue
GTYR15
GSER42
GGLN132
GHOH301

site_idAD6
Number of Residues6
Detailsbinding site for residue CA H 201
ChainResidue
HGLN96
HASP98
HGLU104
HASN119
HASP120
HHOH301

site_idAD7
Number of Residues4
Detailsbinding site for residue NA H 202
ChainResidue
HTYR15
HSER42
HHIS44
HGLN132

site_idAD8
Number of Residues6
Detailsbinding site for residue CA I 201
ChainResidue
IGLN96
IASP98
IGLU104
IASN119
IASP120
IHOH301

site_idAD9
Number of Residues5
Detailsbinding site for residue NA I 202
ChainResidue
ILEU13
ITYR15
ISER42
IHIS44
IGLN132

site_idAE1
Number of Residues7
Detailsbinding site for residue CA J 201
ChainResidue
JHOH301
JHOH302
JGLN96
JASP98
JGLU104
JASN119
JASP120

site_idAE2
Number of Residues5
Detailsbinding site for residue NA J 202
ChainResidue
JLEU13
JTYR15
JSER42
JHIS44
JGLN132

Functional Information from PROSITE/UniProt
site_idPS00615
Number of Residues26
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CVelvsntgyrl..WNDQVCeskna.FLC
ChainResidueDetails
ACYS106-CYS131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1220
DetailsDomain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsMotif: {"description":"Galactose-binding","evidences":[{"source":"UniProtKB","id":"P21963","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues50
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28003128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F2Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsSite: {"description":"Binds aminoglycoside antibiotics (subunit E')","evidences":[{"source":"PubMed","id":"28003128","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsSite: {"description":"Binds aminoglycoside antibiotics (subunit A and E')","evidences":[{"source":"PubMed","id":"28003128","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsSite: {"description":"Binds aminoglycoside antibiotics (subunit A)","evidences":[{"source":"PubMed","id":"28003128","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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